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Database: UniProt
Entry: E3GXN4_METFV
LinkDB: E3GXN4_METFV
Original site: E3GXN4_METFV 
ID   E3GXN4_METFV            Unreviewed;       286 AA.
AC   E3GXN4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Pyruvate ferredoxin oxidoreductase, beta subunit {ECO:0000313|EMBL:ADP77066.1};
DE            EC=1.2.7.1 {ECO:0000313|EMBL:ADP77066.1};
GN   OrderedLocusNames=Mfer_0263 {ECO:0000313|EMBL:ADP77066.1};
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP77066.1, ECO:0000313|Proteomes:UP000002315};
RN   [1] {ECO:0000313|EMBL:ADP77066.1, ECO:0000313|Proteomes:UP000002315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC   {ECO:0000313|Proteomes:UP000002315};
RX   PubMed=21304736;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
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DR   EMBL; CP002278; ADP77066.1; -; Genomic_DNA.
DR   RefSeq; WP_013413344.1; NC_014658.1.
DR   AlphaFoldDB; E3GXN4; -.
DR   STRING; 523846.Mfer_0263; -.
DR   GeneID; 9961978; -.
DR   KEGG; mfv:Mfer_0263; -.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   OMA; ATGCMEV; -.
DR   OrthoDB; 296931at2157; -.
DR   Proteomes; UP000002315; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03376; TPP_PFOR_porB_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 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:ADP77066.1}; Pyruvate {ECO:0000313|EMBL:ADP77066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002315}.
FT   DOMAIN          40..201
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   286 AA;  31554 MW;  F2DB43461E2E7577 CRC64;
     MNEKELLAPG HRGCAGCGAA IGVKLALRVL GKNTIAVTPT GCLEVMTSPY PETAWRIPWI
     HVAFENAAAV AAGVESALKA KGKDDINVVV FAGDGGTVDI GMQALSGAME RGHNIIYVCY
     DNEAYMNTGI QRSGATPFGA STTTTPPGKK SFGENKQKKN MALIMAAHEI PYVATASISY
     PEDYMRKVKK AMEIDRPSYI HLHQPCTTGW RFPPSKTIEV GRLAVESGAW LLYEIENGEF
     RITYRPVERR PVKEYLKMQG RFKHLTDEEI QKIQDYIDEV CSKLRI
//
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