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Database: UniProt
Entry: H5SM67_9GAMM
LinkDB: H5SM67_9GAMM
Original site: H5SM67_9GAMM 
ID   H5SM67_9GAMM            Unreviewed;       147 AA.
AC   H5SM67;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   ORFNames=HGMM_F49B11C15 {ECO:0000313|EMBL:BAL57253.1};
OS   uncultured Gammaproteobacteria bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=86473 {ECO:0000313|EMBL:BAL57253.1};
RN   [1] {ECO:0000313|EMBL:BAL57253.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL57253.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
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; AP011771; BAL57253.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SM67; -.
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          71..147
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   147 AA;  16007 MW;  B8180D3C4DAEBF19 CRC64;
     MDIRTIKKLL EIIEDSSVAE IEIRSGEESI RITRVSTTTQ IVTQPQVSVP AQPPAATASK
     IAEEAKSEET GHIVRSPMVG IFYRAPAPGA KPFVEVGQRV NVGDVLCIIE AMKILNQIEA
     DKAGVITKIL VENGEPVEYN QPLFVIE
//
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