ID A0A117SLH9_9FIRM Unreviewed; 621 AA.
AC A0A117SLH9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
DE Flags: Fragment;
GN ORFNames=APF81_05410 {ECO:0000313|EMBL:KUO78126.1};
OS Desulfosporosinus sp. BRH_c37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO78126.1, ECO:0000313|Proteomes:UP000053148};
RN [1] {ECO:0000313|EMBL:KUO78126.1, ECO:0000313|Proteomes:UP000053148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO78126.1};
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 (OCT-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:KUO78126.1}.
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DR EMBL; LOEW01000064; KUO78126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SLH9; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000053148; 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};
KW Pyruvate {ECO:0000313|EMBL:KUO78126.1}.
FT DOMAIN 1..251
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 538..620
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUO78126.1"
SQ SEQUENCE 621 AA; 68667 MW; C0044A4BEC44EE11 CRC64;
AHQSLWATRM RTEDMLPILT ELDEAGFFSL EVWGGATFDV CLRFLGEDPW ERLRQIKSRV
KKTPLQMLLR AQSLVGYQHY PDDVVREFVS LSVKNGIDII RIFDALNDVR NMVVPMEAAK
KAGAHVQASV VYTISPVHTI KHYLETATSL AELGADSLCI KDMAGLLTPF KAYELVSLLK
KELGIMIHLH SHYIGGIAVP AYLKAVEAGA DVLDTASVPL AFGASQPPVE TVVRALQDTG
YDTGLDLRQL FRIAKYFEAL RKSRGFERGI TRIPDMRVFE HQVPGGMISN LVSQLEEQGA
LERIHDVLEE IPKVRAELGY PPLVTPTSQI VGTQAVLNVL CGVRYKLVPG EVKAYVRGLY
GRPPASIDLE IQKKIIGVEE PLTVRPADIL EPGLAKAVRD SAELAHSPED VISYAIFPQV
AKKFFEERPS GVLIREETKA TKEAKETKET RTTLLSKEDS KLNLQEIKEL IKIIDETEIS
EFNLESDGMK ISIRKGPSML AGVPVVATAH HEEMERVVAH STVQSSQSIE AFSKVPEQAV
LANTEMITSP MVGTFYSSQS PEAPAFVKVG QQVEVGQPVC IIEAMKLMNE IESEIEGKIL
QILVENGQPV EYGQPLFIIG K
//
