ID F0S027_DESTD Unreviewed; 402 AA.
AC F0S027;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Pyruvate synthase {ECO:0000313|EMBL:ADY73708.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:ADY73708.1};
GN OrderedLocusNames=Dester_1071 {ECO:0000313|EMBL:ADY73708.1};
OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73708.1, ECO:0000313|Proteomes:UP000007102};
RN [1] {ECO:0000313|EMBL:ADY73708.1, ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX PubMed=22675590; DOI=10.4056/sigs.2465574;
RA Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfur-reducer
RT Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT hydrothermal vent.";
RL Stand. Genomic Sci. 5:407-415(2011).
RN [2] {ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002543; ADY73708.1; -; Genomic_DNA.
DR RefSeq; WP_013638660.1; NC_015185.1.
DR AlphaFoldDB; F0S027; -.
DR STRING; 868864.Dester_1071; -.
DR KEGG; dte:Dester_1071; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_002569_5_0_0; -.
DR InParanoid; F0S027; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000007102; Chromosome.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ADY73708.1};
KW Pyruvate {ECO:0000313|EMBL:ADY73708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007102}.
FT DOMAIN 22..247
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 269..376
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 402 AA; 44492 MW; 4E46183D16DA7B98 CRC64;
MRPELIKEVT YVPYSGNMAA AEAMRQINPD VVAAYPITPQ TELMQCFADF VANGLVDSEY
IPVESEHSAM SACVGAAAAG SRAMTATAGP GLAYMWEVLG IASGMRLPIV MTVVNRALSA
PINIHGDQSD MMGARDQGWI MLFSENAEEQ YDNLIQVIRI AEDERTRLPV MIGMDGFVIS
HAIERVRLLP DKAVEEFVGE LKPMYSLLDV DNPVAHGAVA MTDSYMEFKR QQREAMMNAY
KVIREVGKAF EEAFGKKYEH IEAYKTEDAD YILVVTGSAA GTAKYVVDKL REEKGIKVGI
IKIRTFRPFP YYDVMDAIEA SNCKAIGILD RAETFGGASG PLFEEVATAQ HLRRKYYPMT
GFIYGLGGRD TNVHHIEEAI DKVMKLAAGE EVPLVNYLNL KE
//
