ID A0A0F2SK24_9FIRM Unreviewed; 628 AA.
AC A0A0F2SK24;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN ORFNames=VR66_06345 {ECO:0000313|EMBL:KJS49812.1};
OS Peptococcaceae bacterium BRH_c23.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS49812.1, ECO:0000313|Proteomes:UP000033503};
RN [1] {ECO:0000313|EMBL:KJS49812.1, ECO:0000313|Proteomes:UP000033503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS49812.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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:KJS49812.1}.
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DR EMBL; LADV01000072; KJS49812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2SK24; -.
DR PATRIC; fig|1629714.3.peg.4447; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000033503; 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:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267}.
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 551..627
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 628 AA; 69479 MW; 4E9FEBDE289DD8D5 CRC64;
MIPVKITDTT LRDAHQSLWA TRMRTEDMVP ILADMDDMGF FSMEVWGGAT FDVCMRFLGE
DPWERLREIK RHVHKTPLQM LLRAQSLVGY QHYPDDVVRE FVALSVKNGI DIIRIFDSLN
DVRNMVVPMQ AAKMAGAHVQ ASVVYTISPV HTTKHYLETA TALADLGADS LCIKDMAGLL
TPFKAYELVS LLKKELGIMI HLHSHYIGGM AVGTYLKAVE AGADVIDTAS VPLAFGASQP
PVETVVRAFQ DTGYDSGLSL RKLFRIAKYF ESLRKSRGFE RGITRISDMR VFEHQVPGGM
ISNLVSQLEE QGALERIHEV LEEIPKVRAE LGFPPLVTPT SQIVGTQAVL NVLSGSRYKL
IPGEVKAYVR GLYGRPPAPI NTDIQKKIIG DEEPMTVRPA DKLEPGLPKA VKDSEGLTRS
PEDVISYALF PQIAKKFFEE RNQGVRAKEE LKNVEETKTT WLSKEDPNLN LQEIKELIQI
IDATEISELN LESDGVKISI RKGPSMVASV PVTATARQEH RALVAADSVQ VSPSVEAETA
KAPEPVVKAN TEIISAPMVG TFYSSQSPDA EAFIKVGQMV EVGQTVCIVE AMKLMNEIES
EFKGKVIQIL VENGQPVEYG QPLFVIEK
//
