ID Q6Q933_9GAMM Unreviewed; 134 AA.
AC Q6Q933;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN ORFNames=Red20E09_31 {ECO:0000313|EMBL:AAS73060.1};
OS uncultured marine gamma proteobacterium EBAC20E09.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster;
OC environmental samples.
OX NCBI_TaxID=266134 {ECO:0000313|EMBL:AAS73060.1};
RN [1] {ECO:0000313|EMBL:AAS73060.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15305915; DOI=10.1111/j.1462-2920.2004.00676.x;
RA Sabehi G., Beja O., Suzuki M.T., Preston C.M., DeLong E.F.;
RT "Different SAR86 subgroups harbour divergent proteorhodopsins.";
RL Environ. Microbiol. 6:903-910(2004).
RN [2] {ECO:0000313|EMBL:AAS73060.1}
RP NUCLEOTIDE SEQUENCE.
RA Sabehi G., Beja O.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU364072}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|RuleBase:RU364072}.
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DR EMBL; AY552545; AAS73060.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6Q933; -.
DR UniPathway; UPA00094; -.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR001249; AcCoA_biotinCC.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00531; BCCP; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR PRINTS; PR01071; ACOABIOTINCC.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|RuleBase:RU364072};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364072}.
FT DOMAIN 58..134
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 134 AA; 14978 MW; 93AD0244FCA26525 CRC64;
MLEESNLNEI EVSQGDESVR ISKGKDPLDY IENNQINTSI SSQEKVSKNE DETRKFIGNQ
VKAPLVGTFY RKPSPDSDPF IKVGDIVKKG QVLCIIEAMK IMNEIKSEFD GEVSSIEIED
GQPVEFGQTI IVIQ
//