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Database: UniProt
Entry: A3CZT6_SHEB5
LinkDB: A3CZT6_SHEB5
Original site: A3CZT6_SHEB5 
ID   A3CZT6_SHEB5            Unreviewed;       149 AA.
AC   A3CZT6;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   OrderedLocusNames=Sbal_0469 {ECO:0000313|EMBL:ABN59999.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN59999.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN59999.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) 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; CP000563; ABN59999.1; -; Genomic_DNA.
DR   RefSeq; WP_011845668.1; NC_009052.1.
DR   AlphaFoldDB; A3CZT6; -.
DR   STRING; 325240.Sbal_0469; -.
DR   KEGG; sbl:Sbal_0469; -.
DR   HOGENOM; CLU_016733_3_1_6; -.
DR   OMA; IKSPIIG; -.
DR   OrthoDB; 9811735at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001557; Chromosome.
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          63..149
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   149 AA;  16221 MW;  C7BCD1739EEC7511 CRC64;
     MAMDLRKIKK LIELVQESDI AELAITEGEE SIRITRYSPM PANVQSSQTL PTVRVAPLNT
     QAKQTAVSPS AEGFVQVSPM VGTFYAAAEL DDVPLVKVGQ KVSQGEVVCI IEAMRMMNPI
     QAERDGVVSA IWAKDGDEVA FDQPLFTLI
//
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