| Identifier | FFH4HYDRLASE [View Relations] [View Alignment]
|
| Accession | PR01575 |
| No. of Motifs | 6 |
| Creation Date | 19-SEP-2001 |
| Title | Formyltetrahydrofolate deformylase signature |
| Database References |
PDB; 1GRC
SCOP; 1GRC
CATH; 1GRC
|
| Literature References | 1. NAGY, P.L., MCCORKLE, G.M. AND ZALKIN, H.
purU, a source of formate for purT-dependent phosphoribosyl-N-formyl-
glycinamide synthesis.
J.BACTERIOL. 175 7066-7073 (1993).
2. NAGY, P.L., MAROLEWSKI, A., BENKOVIC, S.J. AND ZALKIN, H.
Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to
balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts
in Escherichia coli.
J.BACTERIOL. 177 1292-1298 (1995).
|
| Documentation | An Escherichia coli gene designated purU has been identified and
characterised [1]. The gene codes for a 280-amino-acid protein, PurU, whose
C-terminal segment (residues 84-280) exhibits 27% identity with 5'-
phosphoribosylglycinamide (GAR) transformylase, the product of purN [1].
PurU is an enzyme that catalyses the hydrolysis of 10-formyltetrahydrofolate
(formyl-FH4) to FH4 and formate [2]:
10-FORMYLTETRAHYDROFOLATE + H(2)O = FORMATE + TETRAHYDROFOLATE
Formyl-FH4 hydrolase generates the formate that is used by purT-encoded
5'-phosphoribosylglycinamide transformylase for step three of de novo purine
nucleotide synthesis [2]. Formyl-FH4 hydrolase, a hexamer of 32kDa subunits,
is activated by methionine and inhibited by glycine [2]. Heterotropic
cooperativity is observed for activation by methionine in the presence of
glycine and for inhibition by glycine in the presence of methionine [2].
These results suggest that formyl-FH4 hydrolase is a regulatory enzyme whose
main function is to balance the pools of FH4 and C1-FH4 in response to
changing growth conditions [2]. The enzyme uses methionine and glycine to
sense the pools of C1-FH4 and FH4, respectively [2].
FFH4HYDRLASE is a 6-element fingerprint that provides a signature for
formyltetrahydrofolate deformylase. The fingerprint was derived from an
initial alignment of 6 sequences: the motifs were drawn from conserved
regions spanning the full alignment length. Six iterations on
SPTR39.22_17.3f were required to reach convergence, at which point a true
set comprising 18 sequences was identified. Several partial matches were
also found, all of which are formyltetrahydrofolate deformylases and puru-
like proteins that fail to make significant matches with one or more motifs.
|
| Summary Information | 18 codes involving 6 elements
3 codes involving 5 elements
1 codes involving 4 elements
1 codes involving 3 elements
1 codes involving 2 elements
|
| Composite Feature Index | | 6 | 18 | 18 | 18 | 18 | 18 | 18 | | 5 | 2 | 1 | 3 | 3 | 3 | 3 | | 4 | 1 | 1 | 1 | 1 | 0 | 0 | | 3 | 0 | 0 | 1 | 0 | 1 | 1 | | 2 | 1 | 0 | 0 | 1 | 0 | 0 | | 1 | 2 | 3 | 4 | 5 | 6 |
|
| True Positives | O25975 O34990 O67681 PURU_CORSP
PURU_ECOLI PURU_HAEIN PURU_MYCTU PURU_SHIFL
PURU_SYNY3 Q9A2D5 Q9CMF6 Q9HW87
Q9K7U4 Q9KQK6 Q9PCF0 Q9RWT1
Q9X7F7 Q9ZJI2 |
| True Positive Partials | |
| Sequence Titles | O25975 FORMYLTETRAHYDROFOLATE HYDROLASE (PURU) - Helicobacter pylori (Campylobacter pylori).
O34990 YKKE - Bacillus subtilis.
O67681 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Aquifex aeolicus.
PURU_CORSP FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Corynebacterium sp. (strain P-1).
PURU_ECOLI FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Escherichia coli.
PURU_HAEIN FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Haemophilus influenzae.
PURU_MYCTU FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Mycobacterium tuberculosis.
PURU_SHIFL FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Shigella flexneri.
PURU_SYNY3 FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) (FORMYL-FH(4) HYDROLASE) - Synechocystis sp. (strain PCC 6803).
Q9A2D5 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Caulobacter crescentus.
Q9CMF6 PURU - Pasteurella multocida.
Q9HW87 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Pseudomonas aeruginosa.
Q9K7U4 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Bacillus halodurans.
Q9KQK6 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Vibrio cholerae.
Q9PCF0 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Xylella fastidiosa.
Q9RWT1 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Deinococcus radiodurans.
Q9X7F7 PURU PROTEIN - Methylobacterium sp. (strain CM4).
Q9ZJI2 FORMYLTETRAHYDROFOLATE HYDROLASE - Helicobacter pylori J99 (Campylobacter pylori J99).
Q9AGP9 PUTATIVE FORMYLTETRAHYDROFOLATE DEFORMYLASE - Arthrobacter globiformis.
Q9HTE4 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Pseudomonas aeruginosa.
Q9PPC9 FORMYLTETRAHYDROFOLATE DEFORMYLASE (EC 3.5.1.10) - Campylobacter jejuni.
O06440 PURU-LIKE PROTEIN - Rhodobacter capsulatus (Rhodopseudomonas capsulata).
O23579 FORMYLTRANSFERASE PURU HOMOLOG - Arabidopsis thaliana (Mouse-ear cress).
Q9HNU0 FORMYLTETRAHYDROFOLATE DEFORMYLASE - Halobacterium sp. (strain NRC-1).
|
| Scan History | SPTR39.22_17.3f 6 100 NSINGLE
|
| Initial Motifs | Motif 1 width=27
Element Seqn Id St Int Rpt
LRTICPDQKGLIARITNICYKHELNIV PURU_SHIFL 9 9 -
LRTICPDQKGLIARITNICYKHELNIV PURU_ECOLI 9 9 -
LLTDCPDDKGLIAKITNICYKHQLNIL PURU_HAEIN 7 7 -
LLVSCPDQPGIVAQIAQFIYQNQGNII PURU_SYNY3 8 8 -
LLLRCHDRPGIIAAVSTFLARAGANII PURU_MYCTU 33 33 -
LTLQCPEGIGIVHAVTGFLVRHQRTIV PURU_CORSP 9 9 -
Motif 2 width=13
Element Seqn Id St Int Rpt
VDHLTGRFFMRTE PURU_SHIFL 41 5 -
VDHRTGRFFMRTE PURU_ECOLI 41 5 -
VDFETKHFFMRTE PURU_HAEIN 39 5 -
TDFSSGLFLNRVE PURU_SYNY3 40 5 -
TAPEGGTFLQRAI PURU_MYCTU 66 6 -
DDMSAGRLFLRVD PURU_CORSP 41 5 -
Motif 3 width=23
Element Seqn Id St Int Rpt
RIVILVTKEAHCLGDLLMKANYG PURU_SHIFL 86 32 -
RIVILVTKEAHCLGDLLMKANYG PURU_ECOLI 86 32 -
RIVILVTKEAHCLGDILMKNYYG PURU_HAEIN 84 32 -
RLALWVSKQDHCLLDILWRWRSG PURU_SYNY3 90 37 -
RVAIMASTEDHCLLDLLWRNRRG PURU_MYCTU 117 38 -
KVLIMVSKFEHCLQDLLFRMHSG PURU_CORSP 91 37 -
Motif 4 width=28
Element Seqn Id St Int Rpt
GGLDVEIAAVIGNHDTLRSLVERFDIPF PURU_SHIFL 108 -1 -
GGLDVEIAAVIGNHDTLRSLVERFDIPF PURU_ECOLI 108 -1 -
GALDVEIAAVIGNHDNLRELVERFNIPF PURU_HAEIN 106 -1 -
GELRCEIPLIISNHPDLKSIADQFGIDF PURU_SYNY3 112 -1 -
GELEMSVVMVIANHPDLAAHVRPFGVPF PURU_MYCTU 139 -1 -
GDLPIEVVGVASNHPDHRSLVEWYGIGF PURU_CORSP 113 -1 -
Motif 5 width=23
Element Seqn Id St Int Rpt
QDVIHVDHTYTAEDMMRAGRDVE PURU_SHIFL 232 96 -
QDVIHVDHTYTAEDMMRAGRDVE PURU_ECOLI 232 96 -
QNVINVDHTYNAEAMMRAGRDVE PURU_HAEIN 230 96 -
QDVVRVSHRDNVDDLIRKGRDLE PURU_SYNY3 235 95 -
QDVVRVDHTHTVDDLVRVGADVE PURU_MYCTU 262 95 -
QQVVEVDHTYGPQDLVAAGRDSE PURU_CORSP 237 96 -
Motif 6 width=26
Element Seqn Id St Int Rpt
EKNVLSRALYKVLAQRVFVYGNRTII PURU_SHIFL 254 -1 -
EKNVLSRALYKVLAQRVFVYGNRTII PURU_ECOLI 254 -1 -
EKTVLSRALDLALHDRIFVYKNKTVV PURU_HAEIN 252 -1 -
ERVVLARAVRLHLQHRILVYDNRTVV PURU_SYNY3 257 -1 -
ERAVLSRAVLWHCQDRVIVHHNQTIV PURU_MYCTU 284 -1 -
ECKALSNAVRWHCEGRVFLYGNRTVV PURU_CORSP 259 -1 -
|
| Final Motifs | Motif 1 width=27
Element Seqn Id St Int Rpt
LRTICPDQKGLIARITNICYKHELNIV PURU_SHIFL 9 9 -
LRTICPDQKGLIARITNICYKHELNIV PURU_ECOLI 9 9 -
LLTDCPDDKGLIAKITNICYKHQLNII Q9CMF6 7 7 -
LLTDCPDDKGLIAKITNICYKHQLNIL PURU_HAEIN 7 7 -
LLISCHDQPGIVAAISTFLNHHGANIV Q9K7U4 11 11 -
LVIACPDGVGIVAKVSNFLATYNGWIT Q9HW87 6 6 -
LLTHCPDAPGLISKITNICYKHQLNII Q9KQK6 6 6 -
LTISCADQPGIVAAVSQFLHNHGANII Q9RWT1 20 20 -
LLVSCPDQPGIVSAVSAFLFEHGANII O34990 22 22 -
LKIQAKDSKGLVSAISATIANKGYNIV Q9ZJI2 6 6 -
LKIQARDSKGLVSTISTTIANKGYNIV O25975 6 6 -
LLVSCPDQPGIVAQIAQFIYQNQGNII PURU_SYNY3 8 8 -
LTLSCPDQRGIVAKVSAFLFERGCNIL Q9A2D5 3 3 -
LLVSCPDRKGLVKEISSFIADNGGNIV O67681 6 6 -
LLLRCHDRPGIIAAVSTFLARAGANII PURU_MYCTU 33 33 -
LKISCADRPGIVAAVSGALLERDCNIV Q9X7F7 8 8 -
LTLQCPEGIGIVHAVTGFLVRHQRTIV PURU_CORSP 9 9 -
LTLSCPDCTGLVYRISGELFRAGCNIL Q9PCF0 7 7 -
Motif 2 width=13
Element Seqn Id St Int Rpt
VDHLTGRFFMRTE PURU_SHIFL 41 5 -
VDHRTGRFFMRTE PURU_ECOLI 41 5 -
VDFDTKHFFMRTE Q9CMF6 39 5 -
VDFETKHFFMRTE PURU_HAEIN 39 5 -
TDPEGGRFFMRVE Q9K7U4 44 6 -
SDNDNGWFFMRHE Q9HW87 38 5 -
VDNASGHFFMRTE Q9KQK6 38 5 -
TDPAGGQFFMRME Q9RWT1 53 6 -
TDPEGGRFFLRIE O34990 55 6 -
VDPLKQRFFMRLK Q9ZJI2 38 5 -
VDPLKQRFFMRLK O25975 38 5 -
TDFSSGLFLNRVE PURU_SYNY3 40 5 -
DDQETGQFFMRVV Q9A2D5 35 5 -
IDEQTKTFLARVE O67681 38 5 -
TAPEGGTFLQRAI PURU_MYCTU 66 6 -
EDVIEKRFFMRVV Q9X7F7 40 5 -
DDMSAGRLFLRVD PURU_CORSP 41 5 -
GDKESHLFFLRVH Q9PCF0 39 5 -
Motif 3 width=23
Element Seqn Id St Int Rpt
RIVILVTKEAHCLGDLLMKANYG PURU_SHIFL 86 32 -
RIVILVTKEAHCLGDLLMKANYG PURU_ECOLI 86 32 -
RIVILVTKEAHCLGDILMKNYYG Q9CMF6 84 32 -
RIVILVTKEAHCLGDILMKNYYG PURU_HAEIN 84 32 -
RMAIFVSKEDHCLLELLWKWHSN Q9K7U4 94 37 -
RVVLMASKESHCLADLLHRWHSG Q9HW87 88 37 -
RIVILVTKEAHCLGDILMKNYDG Q9KQK6 83 32 -
KMAVLVSRYDHCFLDLLWRRRRG Q9RWT1 104 38 -
RVAIFVSKNLHCLHELIWEWQTG O34990 105 37 -
NIILLATKESHCLGDLLLRVYGG Q9ZJI2 95 44 -
NIILLATKESHCLGDLLLRVYGG O25975 95 44 -
RLALWVSKQDHCLLDILWRWRSG PURU_SYNY3 90 37 -
RVLLLASKFDHCLADLVYRWRIG Q9A2D5 83 35 -
KVAIFVSKQEHCFYDLMHRFYSG O67681 88 37 -
RVAIMASTEDHCLLDLLWRNRRG PURU_MYCTU 117 38 -
RVMILVSRFDHCLVDILYRKRIG Q9X7F7 90 37 -
KVLIMVSKFEHCLQDLLFRMHSG PURU_CORSP 91 37 -
RLLVMVSKQGHCLNDLLFRIHSR Q9PCF0 88 36 -
Motif 4 width=28
Element Seqn Id St Int Rpt
GGLDVEIAAVIGNHDTLRSLVERFDIPF PURU_SHIFL 108 -1 -
GGLDVEIAAVIGNHDTLRSLVERFDIPF PURU_ECOLI 108 -1 -
GGLDVEIAAVIGNHDTLRTLVERFDIPF Q9CMF6 106 -1 -
GALDVEIAAVIGNHDNLRELVERFNIPF PURU_HAEIN 106 -1 -
NELICDIPLVISNHDELRDVVEGYGIPY Q9K7U4 116 -1 -
GELDCEIPCVIANHDDLRSMVEWHGIPY Q9HW87 110 -1 -
GSLDVDIAAVVGNYDTLQRLTERFDIPY Q9KQK6 105 -1 -
GELNVEIPLILSNHEDLRRDAEMFGIPF Q9RWT1 126 -1 -
GNLMAEIAVVISNHEEARELVERLNIPF O34990 127 -1 -
GELNAQILGVISNHEILRPLVEKFDIPY Q9ZJI2 117 -1 -
GELNAQILGVISNHEILRPLVEKFDIPY O25975 117 -1 -
GELRCEIPLIISNHPDLKSIADQFGIDF PURU_SYNY3 112 -1 -
GELPMDITGVVSNHPAQTYAHVDLSGLD Q9A2D5 105 -1 -
GELKGEVKLVISNHEKARKTAEFFGVPF O67681 110 -1 -
GELEMSVVMVIANHPDLAAHVRPFGVPF PURU_MYCTU 139 -1 -
GELPMDLTAVVTNHAAENYAHLDLCGAP Q9X7F7 112 -1 -
GDLPIEVVGVASNHPDHRSLVEWYGIGF PURU_CORSP 113 -1 -
RQLQAKIVTVVSNHNDFAPLTASYGVPF Q9PCF0 110 -1 -
Motif 5 width=23
Element Seqn Id St Int Rpt
QDVIHVDHTYTAEDMMRAGRDVE PURU_SHIFL 232 96 -
QDVIHVDHTYTAEDMMRAGRDVE PURU_ECOLI 232 96 -
QNVINVDHTYNAEAMMRAGRDVE Q9CMF6 230 96 -
QNVINVDHTYNAEAMMRAGRDVE PURU_HAEIN 230 96 -
QDVLRVNHRYSVPQLRVAGRNVE Q9K7U4 240 96 -
QDVVRVTHRDNVEDMVRLGKDVE Q9HW87 234 96 -
QDVIPVDHTFSAQDMAQAGRDVE Q9KQK6 229 96 -
QDVIPVTHRETPDTLMRMGRDVE Q9RWT1 250 96 -
QDIKRVDHRDNAETLKNIGRTIE O34990 251 96 -
QDTLPINHNYSVEKMRLAGKDIE Q9ZJI2 245 100 -
QDTLPINHNYSVEKMRLAGKDIE O25975 245 100 -
QDVVRVSHRDNVDDLIRKGRDLE PURU_SYNY3 235 95 -
QDVERISHRDTPEDLVRKGRDIE Q9A2D5 230 97 -
QDVVRVSHKDSLEDFIRKGKDIE O67681 234 96 -
QDVVRVDHTHTVDDLVRVGADVE PURU_MYCTU 262 95 -
QDVERISHSDSPEDLVRKGRDIE Q9X7F7 237 97 -
QQVVEVDHTYGPQDLVAAGRDSE PURU_CORSP 237 96 -
QDVARVDHSMTAHDLVRIGSDIE Q9PCF0 234 96 -
Motif 6 width=26
Element Seqn Id St Int Rpt
EKNVLSRALYKVLAQRVFVYGNRTII PURU_SHIFL 254 -1 -
EKNVLSRALYKVLAQRVFVYGNRTII PURU_ECOLI 254 -1 -
EKTVLSRALDLALHDRIFVYKNKTVV Q9CMF6 252 -1 -
EKTVLSRALDLALHDRIFVYKNKTVV PURU_HAEIN 252 -1 -
ERVVLARAVNWYLEDKIIVYSNKTVV Q9K7U4 262 -1 -
EKLVLARGLRYHLEDRVLVHGNKTVV Q9HW87 256 -1 -
EKNVLSKALNKVLNDHVFVYGNKTVI Q9KQK6 251 -1 -
ERQVLARAVKAHVEDRVLVYGNKTVV Q9RWT1 272 -1 -
ERSVLARAVKWHLEDRVIVHENKTIV O34990 273 -1 -
EKLVLARALKLVLEDRVFVHENKTVV Q9ZJI2 267 -1 -
EKLVLARALKLVLEDRVFVHENKTVV O25975 267 -1 -
ERVVLARAVRLHLQHRILVYDNRTVV PURU_SYNY3 257 -1 -
ERRVLARALRYRLEDRVLLNGRKTVV Q9A2D5 252 -1 -
EKVVLARAVKWHLEDKILVYNGKTVV O67681 256 -1 -
ERAVLSRAVLWHCQDRVIVHHNQTIV PURU_MYCTU 284 -1 -
ERRVLARALRYHLDDRVLLNGHKTVV Q9X7F7 259 -1 -
ECKALSNAVRWHCEGRVFLYGNRTVV PURU_CORSP 259 -1 -
ESLVLARAVSRHIEHRILLNGHRTVV Q9PCF0 256 -1 -
|