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Database: UniProt
Entry: F3PN75_9BACE
LinkDB: F3PN75_9BACE
Original site: F3PN75_9BACE 
ID   F3PN75_9BACE            Unreviewed;       611 AA.
AC   F3PN75;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Biotin-requiring enzyme {ECO:0000313|EMBL:EGF59867.1};
GN   ORFNames=HMPREF9446_00161 {ECO:0000313|EMBL:EGF59867.1};
OS   Bacteroides fluxus YIT 12057.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59867.1, ECO:0000313|Proteomes:UP000003416};
RN   [1] {ECO:0000313|EMBL:EGF59867.1, ECO:0000313|Proteomes:UP000003416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59867.1,
RC   ECO:0000313|Proteomes:UP000003416};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:EGF59867.1}.
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DR   EMBL; AFBN01000004; EGF59867.1; -; Genomic_DNA.
DR   RefSeq; WP_009123527.1; NZ_GL882605.1.
DR   AlphaFoldDB; F3PN75; -.
DR   STRING; 763034.HMPREF9446_00161; -.
DR   eggNOG; COG0511; Bacteria.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_2_10; -.
DR   Proteomes; UP000003416; Unassembled WGS sequence.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000003416}.
FT   DOMAIN          4..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          526..611
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   611 AA;  67905 MW;  9CD6040C0E943E1A CRC64;
     MKKEIKFSLV FRDMWQSAGK YVPRVDQLVK VAPAIIEMGC FARVETNGGG FEQVNLLFGE
     NPNKAVREWT KPFHEAGIQT HMLDRALNGL RMSPVPADVR KLFYKVKKAQ GTDITRTFCG
     LNDVRNIIPS ITYAKEAGMI SQCSLCITHS PIHTVEYYTD MALKLIKAGA DEICIKDMAG
     IGRPVSLGKI VANIKAAHPD IPVQYHSHAG PGFNMASILE VCEAGCDYID VGMEPLSWGT
     GHADLLSVQA MLKDAGFQVP EINMEAYMKV RALIQEFMDD FLGLYISPKN RLMNSLLIAP
     GLPGGMMGSL MADLETNLES INKYKAKRNL PFMTQDQLLI KLFNEVAYVW PRVGYPPLVT
     PFSQYVKNLS MMNVIAMEKG KERWGMIADD IWDMLLGKAG KLPGQLAPEI IEKAEREGRK
     FFTGNPQDNY PDALDKYRKM MKENKWESGE DDEELFEYAM HPAQYEAYKS GKAKEDFLAD
     VEKRRAERDK SPLDDAKPKT LTVQVDGQAY RVTVAYGDID LPASATEKVT APVGEGQDVP
     APLEGKFFLT KNAQETPLKV GDKVAKGDLL CYIEAMKTYN AIRADFAGTV TAICVNPGDS
     VSEDDVLMKI G
//
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