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Database: UniProt
Entry: Q6Q933_9GAMM
LinkDB: Q6Q933_9GAMM
Original site: Q6Q933_9GAMM 
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
//
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