ID G2FMD7_9FIRM Unreviewed; 618 AA.
AC G2FMD7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN ORFNames=DOT_0845 {ECO:0000313|EMBL:EGW41205.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41205.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW41205.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW41205.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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:EGW41205.1}.
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DR EMBL; AGAF01000043; EGW41205.1; -; Genomic_DNA.
DR RefSeq; WP_009614327.1; NZ_AGAF01000043.1.
DR AlphaFoldDB; G2FMD7; -.
DR PATRIC; fig|913865.3.peg.787; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000004928; 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 535..617
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 618 AA; 67965 MW; F02C945BF6D5403B CRC64;
MKPVKITDTT LRDAHQSLWA TRMRTEDMLP ILADLDEVGF FSLEVWGGAT FDVCLRFLGE
DPWERLRQIK RRVKKTPLQM LLRGQSLVGY THYSDDVVRE FVALSVKNGI DIIRIFDALN
DVRNMVVPIQ AAKQAGAHVQ ASVVYTISPV HTLKHYLETA TALAELGADS ICIKDMAGLL
TPFKAFEMVK LLKKELGIMI HLHSHYIGGM AVGTYLKAAE AGVDVIDSAS VPLAFGASQP
PVETVVRAFE GTEYDTGLNL HQLFQIAEYF ETHRKKRGFD RGITRISDMK VFEHQVPGGM
ITNFITQLEE QKAMDRIYDV LEEVPKVRAE LGYPPLVTPT SQIVGTQAVL NVLSGARYKL
VPAEVKAYVR GLYGRSPAPI DPEIQKKIIG DEEPLTVRPA DVLEPGLAKA ERESAGFACS
PEDVISYALF PQIAKKFFEE RKMGVSLKEE LPETPKIQPQ LLTKEDSKLN LDDIKELIKS
VNETEISELN FEKEGLKVSI SKGSSGAAGI PVMAPPPVPQ KAIGMEVGPA NAPESVVLGV
TETITSPMVG TFYQAPSSDA APYVKLGLQV KVGQPVCIIE AMKLMNEIEA DAAGKIVKIM
VKDGQPVEYG QPLFVIEK
//