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PR01071

Identifier
ACOABIOTINCC  [View Relations]  [View Alignment]  
Accession
PR01071
No. of Motifs
3
Creation Date
18-FEB-1999  (UPDATE 06-JUN-1999)
Title
Acetyl-CoA biotin carboxyl carrier protein signature
Database References

PROSITE; PS00188 BIOTIN
BLOCKS; BL00188
PFAM; PF00364 biotin_req_enzy
INTERPRO; IPR001249
PDB; 1BDO
SCOP; 1BDO
CATH; 1BDO
Literature References
1. STRYER, L.
Fatty Acid Metabolism.
IN BIOCHEMISTRY 3RD ED., W.H. FREEMAN AND CO. (NEW YORK), 1988, PP.480-485.
 
2. LI, J.J. AND CRONAN, J.E.
The gene encoding the biotin carboxylase subunit of Escherichia coli
acetyl-CoA caboxylase.
J.BIOL.CHEM. 267(24) 855-63 (1992).
 
3. LI, J.J. AND CRONAN, J.E.
The genes encoding the two carboxyl transferase subunits of Escherichia
coli acetyl-CoA carboxylase.
J.BIOL.CHEM. 267(24) 16841-16847 (1992).
 
4. ATHAPPILLY, F.K. AND HENDRICKSON, W.A.
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase
determined by MAD phasing.
STRUCTURE 3(12) 1407-19 (1995).

Documentation
Fatty acid synthesis involves a set of reactions, commencing with 
carboxylation of acetyl-CoA to malonyl-CoA [1]. This is an irreversible
reaction, catalysed by the acetyl-CoA carboxylase complex (EC 6.4.1.2); a
heterohexamer of biotin carboxyl carrier protein, biotin carboxylase [2] and
two non-identical carboxyl transferase subunits (alpha and beta) in a 2:2
association [1,3]. 
 
The reaction involves two steps: 
 
(1) Biotin carrier protein + ATP + HCO(3)(-) <=>
	    Carboxybiotin carrier protein + ADP + Phosphate
 
(2) Carboxybiotin carrier protein + Acetyl-CoA ->
	    Malonyl-CoA + Biotin carrier protein
 
In the first step, biotin carboxylase catalyses the carboxylation of the
carrier protein to form an intermediate. Next, the transcarboxylase complex
transfers the carboxyl group from the intermediate to acetyl-CoA forming
malonyl-CoA.
 
The crystal structure of selenomethionyl (Se-met) biotin carboxy carrier 
protein has been determined to 1.8A resolution [4]. The structure forms a
capped beta sandwich with quasi-dyad symmetry, each half of which contains
a characteristic hammerhead motif [4]. The biotinylated lysine is located at
a hairpin beta-turn that connects the symmetric halves of the molecule, and
its biotinyl group interacts with a non-symmetric protrusion from the core.
The hammerhead domain is regarded as the basic structural motif of biotinyl
and lipoyl domains of a superfamily of enzymes [4].
 
ACOABIOTINCC is a 3-element fingerprint that provides a signature for the
acetyl-CoA biotin carboxyl carrier protein. The fingerprint was derived from
an initial alignment of 7 sequences: the motifs were drawn from conserved
regions within the C-terminal portion of the alignment - motif 1 encodes 
beta-strand 2; motif 2 spans strand 3 and the N-terminus of strand 4; and
motif 3 spans the C-terminus of strand 4 and beta-strand 5, and includes the
biotin-binding lysine (motifs 2 and 3 span the region encoded by PROSITE
pattern BIOTIN (PS00188)). Three iterations on OWL31.1 were required to 
reach convergence, at which point a true set comprising 21 sequences was
identified. A single partial match was also found, S66566, a biotin 
carboxyl carrier fragment that matches motifs 2 and 3.
 
An update on SPTR37_9f identified a true set of 18 sequences.
Summary Information
18 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3181818
2000
123
True Positives
BCCP_ANASP    BCCP_ARATH    BCCP_BACSU    BCCP_CYACA    
BCCP_ECOLI BCCP_HAEIN BCCP_PORPU BCCP_PSEAE
BCCP_SOYBN O25135 O67375 O84125
Q39348 Q39349 Q39350 Q54279
Q54761 Q55120
Sequence Titles
BCCP_ANASP  BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - ANABAENA SP. (STRAIN PCC 7120). 
BCCP_ARATH BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE PRECURSOR (BCCP) - ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
BCCP_BACSU BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - BACILLUS SUBTILIS.
BCCP_CYACA BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - CYANIDIUM CALDARIUM (GALDIERIA SULPHURARIA).
BCCP_ECOLI BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - ESCHERICHIA COLI.
BCCP_HAEIN BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - HAEMOPHILUS INFLUENZAE.
BCCP_PORPU BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - PORPHYRA PURPUREA.
BCCP_PSEAE BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (BCCP) - PSEUDOMONAS AERUGINOSA.
BCCP_SOYBN BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE PRECURSOR (BCCP) - GLYCINE MAX (SOYBEAN).
O25135 BIOTIN CARBOXYL CARRIER PROTEIN (FABE) - HELICOBACTER PYLORI (CAMPYLOBACTER PYLORI).
O67375 BIOTIN CARBOXYL CARRIER PROTEIN - AQUIFEX AEOLICUS.
O84125 BIOTIN CARBOXYL CARRIER PROTEIN - CHLAMYDIA TRACHOMATIS.
Q39348 BIOTIN CARBOXYL CARRIER PROTEIN - BRASSICA NAPUS (RAPE).
Q39349 BIOTIN CARBOXYL CARRIER PROTEIN - BRASSICA NAPUS (RAPE).
Q39350 BIOTIN CARBOXYL CARRIER PROTEIN - BRASSICA NAPUS (RAPE).
Q54279 BIOTIN CARBOXYL CARRIER PROTEIN - SACCHAROPOLYSPORA HIRSUTA.
Q54761 BIOTIN CARBOXYL CARRIER PROTEIN - SYNECHOCOCCUS SP. (STRAIN PCC 7942) (ANACYSTIS NIDULANS R2).
Q55120 BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
Scan History
OWL31_1    3  45   NSINGLE    
SPTR37_9f 2 28 NSINGLE
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
SPMAGTFYRSPAPG BCCP_SOYBN 190 190 -
SPMAGTFYRSPAPG BCCP_ARATH 208 208 -
SPMVGTFYRAPAPG BCCP_ANASP 108 108 -
SPMVGTFYHSPAPG BCCP_PORPU 85 85 -
SPMVGTFYRSPSPE BCCP_HAEIN 84 84 -
SPMVGTFYRTPSPD BCCP_ECOLI 85 85 -
SPMVGTFYASSSPE BCCP_BACSU 86 86 -

Motif 2 width=15
Element Seqn Id St Int Rpt
FVKVGDKVKKGQVVC BCCP_SOYBN 207 3 -
FIKVGDKVQKGQVLC BCCP_ARATH 225 3 -
FVEVGDRIRQGQTVC BCCP_ANASP 125 3 -
FVQVGDIVKCNQTVC BCCP_PORPU 102 3 -
FVEVGQSVKVGDALC BCCP_HAEIN 101 3 -
FIEVGQKVNVGDTLC BCCP_ECOLI 102 3 -
YVTAGSKVNENTVVC BCCP_BACSU 103 3 -

Motif 3 width=14
Element Seqn Id St Int Rpt
IIEAMKLMNEIEAD BCCP_SOYBN 222 0 -
IVEAMKLMNEIESD BCCP_ARATH 240 0 -
IIEAMKLMNEIEAD BCCP_ANASP 140 0 -
IIEAMKLMNEIEAE BCCP_PORPU 117 0 -
IVEAMKMMNRIEAD BCCP_HAEIN 116 0 -
IVEAMKMMNQIEAD BCCP_ECOLI 117 0 -
IVEAMKLFIEIEAE BCCP_BACSU 118 0 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
SPMAGTFYRSPAPG BCCP_SOYBN 190 190 -
SPMAGTFYRSPGPG Q39348 90 90 -
SPMAGTFYRSPGPG Q39350 179 179 -
SPMVGTFYRAPAPD Q55120 82 82 -
SPMAGTFYRSPAPG BCCP_ARATH 208 208 -
SPMVGTFYRAPAPG BCCP_ANASP 108 108 -
SYGLGTFYRSPGPG Q39349 184 184 -
SPMVGTFYHSPAPG BCCP_PORPU 85 85 -
SPLVGTFYRSPAPG O67375 80 80 -
SPMVGTFYRSPSPE BCCP_HAEIN 84 84 -
APMVGTFYRAPAPE Q54761 85 85 -
SPMVGTFYRAASPT BCCP_PSEAE 85 85 -
SPMVGTFYRTPSPD BCCP_ECOLI 85 85 -
SPMVGTFYHAPSPG O25135 83 83 -
SPISGIFYSSSKPG BCCP_CYACA 77 77 -
SPLVGTFYGSPSPE O84125 91 91 -
SPMVGTFYASSSPE BCCP_BACSU 86 86 -
APSVGVFYRAPEPG Q54279 90 90 -

Motif 2 width=15
Element Seqn Id St Int Rpt
FVKVGDKVKKGQVVC BCCP_SOYBN 207 3 -
FVKVGDKVQKGQVVC Q39348 107 3 -
FVKVGDKVQKGQVVC Q39350 196 3 -
FVEVGDAVSKGQGVC Q55120 99 3 -
FIKVGDKVQKGQVLC BCCP_ARATH 225 3 -
FVEVGDRIRQGQTVC BCCP_ANASP 125 3 -
FVKVGDKVQKGQVVC Q39349 201 3 -
FVQVGDIVKCNQTVC BCCP_PORPU 102 3 -
FVEVGDIVSPGQVLC O67375 97 3 -
FVEVGQSVKVGDALC BCCP_HAEIN 101 3 -
FVNVGDRIQVGQTVC Q54761 102 3 -
FVEVGQSVKKGDILC BCCP_PSEAE 102 3 -
FIEVGQKVNVGDTLC BCCP_ECOLI 102 3 -
YVKAGDTLKKGQIVG O25135 100 3 -
FVAVGSVVSKGQTLC BCCP_CYACA 94 3 -
FIKPGDTVSEDTVVC O84125 108 3 -
YVTAGSKVNENTVVC BCCP_BACSU 103 3 -
FVAEGDTIRPGQQVG Q54279 107 3 -

Motif 3 width=14
Element Seqn Id St Int Rpt
IIEAMKLMNEIEAD BCCP_SOYBN 222 0 -
IIEAMKLMNEIEAE Q39348 122 0 -
IIEAMKLMNEIEAE Q39350 211 0 -
IIEAMKLMNEIEAE Q55120 114 0 -
IVEAMKLMNEIESD BCCP_ARATH 240 0 -
IIEAMKLMNEIEAD BCCP_ANASP 140 0 -
IIEAMKLMNEIEAE Q39349 216 0 -
IIEAMKLMNEIEAE BCCP_PORPU 117 0 -
IIEALKVMNEIESD O67375 112 0 -
IVEAMKMMNRIEAD BCCP_HAEIN 116 0 -
ILEAMKLMNELESE Q54761 117 0 -
IVEAMKMMNHIEAE BCCP_PSEAE 117 0 -
IVEAMKMMNQIEAD BCCP_ECOLI 117 0 -
IVEAMKIMNEIEVE O25135 115 0 -
IIEAMKTMNEIESD BCCP_CYACA 109 0 -
IVEAMKVMNEVKAG O84125 123 0 -
IVEAMKLFIEIEAE BCCP_BACSU 118 0 -
IVEAMKLMIPVKSE Q54279 122 0 -