ID Q725S6_DESVH Unreviewed; 245 AA.
AC Q725S6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase, beta subunit, putative {ECO:0000313|EMBL:AAS97817.1};
GN OrderedLocusNames=DVU_3348 {ECO:0000313|EMBL:AAS97817.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS97817.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS97817.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- INTERACTION:
CC Q725S6; Q725S7: DVU_3347; NbExp=5; IntAct=EBI-10065263, EBI-10065266;
CC Q725S6; Q725S5: DVU_3349; NbExp=3; IntAct=EBI-10065263, EBI-10065269;
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DR EMBL; AE017285; AAS97817.1; -; Genomic_DNA.
DR AlphaFoldDB; Q725S6; -.
DR SMR; Q725S6; -.
DR IntAct; Q725S6; 3.
DR STRING; 882.DVU_3348; -.
DR PaxDb; 882-DVU_3348; -.
DR EnsemblBacteria; AAS97817; AAS97817; DVU_3348.
DR KEGG; dvu:DVU_3348; -.
DR eggNOG; COG1013; Bacteria.
DR HOGENOM; CLU_048564_2_1_7; -.
DR PhylomeDB; Q725S6; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF3; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AAS97817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT DOMAIN 51..189
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 245 AA; 26401 MW; 92909DB67BDA2ECE CRC64;
MPELLVDRAT HYCPGCHHGV AHRLVAEVLT EMGVAEDTIC VSSIGCSVFI YNYLAVDTVE
APHGRAPAVA TGVKRARKDK IVFAYQGDGD LASIGLAEIM HAANRGERMT IVFVNNTVYG
MTGGQMAPTT LVGQKTTTCP SGRCRDTEGL PMKMAEIIAG LGGVAYSARV SLDSVKHIRA
AKKALRKAFD VQQNDLGFGF VEMLSACPTN WRMDAVKANK RIAEEMIPYF PLGVYKDVTE
AEGVC
//
