ID A0A0D6XT69_9STAP Unreviewed; 288 AA.
AC A0A0D6XT69;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:KIX91640.1};
DE SubName: Full=Ferredoxin oxidoreductase subunit beta {ECO:0000313|EMBL:SUM57347.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:SUM57347.1};
GN Name=porB {ECO:0000313|EMBL:SUM57347.1};
GN ORFNames=NCTC13832_01021 {ECO:0000313|EMBL:SUM57347.1}, TP70_01480
GN {ECO:0000313|EMBL:KIX91640.1};
OS Staphylococcus microti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=569857 {ECO:0000313|EMBL:KIX91640.1, ECO:0000313|Proteomes:UP000032366};
RN [1] {ECO:0000313|EMBL:KIX91640.1, ECO:0000313|Proteomes:UP000032366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22147 {ECO:0000313|EMBL:KIX91640.1,
RC ECO:0000313|Proteomes:UP000032366};
RA Guo J.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUM57347.1, ECO:0000313|Proteomes:UP000254100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13832 {ECO:0000313|EMBL:SUM57347.1,
RC ECO:0000313|Proteomes:UP000254100};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; JXWY01000007; KIX91640.1; -; Genomic_DNA.
DR EMBL; UHDT01000001; SUM57347.1; -; Genomic_DNA.
DR RefSeq; WP_044358824.1; NZ_UHDT01000001.1.
DR AlphaFoldDB; A0A0D6XT69; -.
DR STRING; 569857.TP70_01480; -.
DR PATRIC; fig|569857.6.peg.2157; -.
DR OrthoDB; 9775140at2; -.
DR Proteomes; UP000032366; Unassembled WGS sequence.
DR Proteomes; UP000254100; Unassembled WGS sequence.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03375; TPP_OGFOR; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR011896; OFOB.
DR InterPro; IPR032686; PFO_beta_C.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR02177; PorB_KorB; 1.
DR PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF12367; PFO_beta_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SUM57347.1}.
FT DOMAIN 48..195
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 199..263
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
SQ SEQUENCE 288 AA; 31306 MW; BEF4ED50C7989125 CRC64;
MATFKDFRNN VKPNWCPGCG DFSVQAAIQK AAANVGLEPD EVALITGIGC SGRLSGYVNS
YGVHSIHGRA LPLAQGVKMA NRDLTVIASG GDGDGYAIGM GHTIHALRRN MNITYIVMDN
QIYGLTKGQT SPSSAPGFVT KTTPKGNIEQ NVAPLELALS SGATFVAQGF SSDIKALTKM
IEDAINHDGF SFVNVFSPCV TYNKVNTYDW FKEHLTDLNE IEDYDTSDKQ RAIQTVVEHN
SLVKGIVYQD TETPSYESQI ETLGETPLAH QNIELTEAQF ESLTKQFV
//