ID Q3ATP2_CHLCH Unreviewed; 157 AA.
AC Q3ATP2;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN OrderedLocusNames=Cag_0360 {ECO:0000313|EMBL:ABB27633.1};
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB27633.1};
RN [1] {ECO:0000313|EMBL:ABB27633.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB27633.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-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|RuleBase:RU364072}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU364072}.
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DR EMBL; CP000108; ABB27633.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3ATP2; -.
DR STRING; 340177.Cag_0360; -.
DR KEGG; cch:Cag_0360; -.
DR eggNOG; COG0511; Bacteria.
DR HOGENOM; CLU_016733_3_1_10; -.
DR OMA; IKSPIIG; -.
DR OrthoDB; 9811735at2; -.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR000551; MerR-type_HTH_dom.
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.
DR PROSITE; PS50937; HTH_MERR_2; 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}.
FT DOMAIN 1..12
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
FT DOMAIN 80..156
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 157 AA; 16804 MW; 2DE21BC010063AE3 CRC64;
MNLSDIKELI DVVNNSDLQE AIIEEGNFKL ILRRPAPVVV QQAAPAAIAP TAMPAPTYAA
PAPQATAPAA KPAPTIDTSL IECRSPIVGT FYHASSPDTP PFVSINDTIK KGDVLCIIEA
MKLMNEIEAE VSGTIVEILV ENGQAVEYDQ PLFRIKP
//