ID   A0A101EA39_9FIRM        Unreviewed;       632 AA.
AC   A0A101EA39;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN   ORFNames=XD50_0650 {ECO:0000313|EMBL:KUK11010.1};
OS   Clostridia bacterium 41_269.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK11010.1, ECO:0000313|Proteomes:UP000053409};
RN   [1] {ECO:0000313|Proteomes:UP000053409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUK11010.1}.
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DR   EMBL; LGEZ01000006; KUK11010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101EA39; -.
DR   STRING; 1635275.XD50_0650; -.
DR   PATRIC; fig|1635275.3.peg.289; -.
DR   Proteomes; UP000053409; 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:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
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   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
FT   DOMAIN          7..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          554..630
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   632 AA;  70890 MW;  2AB96BC17B162F33 CRC64;
     MKKIKKIKIT DTTLRDAHQS LWATRMSTSD MLPIIERLDS LGYYSLETWG GATFDVCMRY
     LNEDPWERLR LLKKYAKKTP LQMLLRGQAL VGYQHYPDDV VESFVAKAVE NGIDIIRIFD
     ALNDLRNMEK SIEVAKREGA HVQGAVVYTV SPVHSTEHYL NVAMQLQEMG VDSICIKDMA
     GLLTPYKAAE LVKPFKEKLS VPIHLHSHYV GGLAFGAYLK GIEAGADGID TASVPLAFGS
     SQPPVETVVR ALEESEFETG LDLHELFEVA NYFEEIRKKH GFQRGVTRIT DMWVFEHQVP
     GGMISNLVNQ LKEQNATDKL EEVLKEIPRV REDLGYPPLV TPTSQIVGTQ AVLNVLTGER
     YKLVPGEVKA YLRGAYGRPP GKINEEIRRK IIGDEEIYEG RPADLLEPGM EKAREEIKDL
     ATCEEDVISY ALFPQVARKF FEEGRKKKKI FAVEQTVAAT REHVAEDEAA DLEQEVGDVR
     ISDIKELLKV LNETGTTEFN YEGDGMRLVV RRGKMILAEE KGEVLSIEQK EQAVSESDEE
     KKVEKEGIEE GEDIVVVEAP MVGTFYRAPA PDADPFVEVG SKVKKGQTLC IIEAMKLFNE
     IETEVDGEVV AILVENGQPV EYGQPLFKIK KG
//