ID C7DD07_9RHOB Unreviewed; 159 AA.
AC C7DD07;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN Name=accB {ECO:0000313|EMBL:EET47091.1};
GN ORFNames=TR2A62_0160 {ECO:0000313|EMBL:EET47091.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET47091.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET47091.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET47091.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) 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|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU364072}.
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DR EMBL; GG697169; EET47091.1; -; Genomic_DNA.
DR RefSeq; WP_009158165.1; NZ_GG697169.2.
DR AlphaFoldDB; C7DD07; -.
DR STRING; 633131.TR2A62_0160; -.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_016733_3_1_5; -.
DR OrthoDB; 9811735at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000004701; Unassembled WGS sequence.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267, 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004701}.
FT DOMAIN 83..159
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 159 AA; 16548 MW; 7E67ADBFD6D7BC46 CRC64;
MTKKNQADSD VDFIQALAAV LRENDLTELQ VKRDYGENDT LNVRVSRQQP QQIVTQVAAA
PAAAAPVAAP AAAEPAADPA SHPGAVTSPM VGTVYMAPEP GAPAFATVGA QINEGDTILI
VEAMKTMNHI PAPKSGTIKR ILVEDGAPVE FGTPLVIVE
//