ID D4H1J6_DENA2 Unreviewed; 273 AA.
AC D4H1J6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit {ECO:0000313|EMBL:ADD68756.1};
GN OrderedLocusNames=Dacet_1993 {ECO:0000313|EMBL:ADD68756.1};
OS Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Geovibrionaceae; Denitrovibrio.
OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD68756.1, ECO:0000313|Proteomes:UP000002012};
RN [1] {ECO:0000313|EMBL:ADD68756.1, ECO:0000313|Proteomes:UP000002012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12809 / NBRC 114555 / N2460
RC {ECO:0000313|Proteomes:UP000002012};
RX PubMed=21304711; DOI=10.4056/sigs.892105;
RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT (N2460).";
RL Stand. Genomic Sci. 2:270-279(2010).
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; CP001968; ADD68756.1; -; Genomic_DNA.
DR RefSeq; WP_013011260.1; NC_013943.1.
DR AlphaFoldDB; D4H1J6; -.
DR STRING; 522772.Dacet_1993; -.
DR PaxDb; 522772-Dacet_1993; -.
DR KEGG; dap:Dacet_1993; -.
DR eggNOG; COG1013; Bacteria.
DR HOGENOM; CLU_048564_0_0_0; -.
DR InParanoid; D4H1J6; -.
DR OrthoDB; 9775140at2; -.
DR Proteomes; UP000002012; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Pyruvate {ECO:0000313|EMBL:ADD68756.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002012}.
FT DOMAIN 47..194
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 198..257
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
SQ SEQUENCE 273 AA; 29642 MW; 8C9EE014ED90B0F9 CRC64;
MKPLDYNTGK IPVWCPGCGN FAIWNSIKKA LASVDMEPHK LALVSGIGCS GKMINHVRSY
GFHALHGRAL PVATGIKLAN PDMTVLVNGG DGDGYGMGIG HLIHAIRRNI DVTYVVHHNK
VYGLTTGQAA PTSPEGTVSK STPFGVVDSQ LNPLILAMAA GATYVARGYS GESDQLAELI
EGGIRHNGFA LIDVLQPCVT FGGEYKYDYY NDRVVKMDEI PSHDKAIELA QDTDHYHLGV
FSQYDRPAYN EQHPEITKGI TAKDVTNLIQ EYV
//