ID F4LRY4_TEPAE Unreviewed; 393 AA.
AC F4LRY4; L0S250;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Pyruvate synthase subunit PorA {ECO:0000313|EMBL:CCP27211.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:CCP27211.1};
GN Name=porA {ECO:0000313|EMBL:CCP27211.1};
GN OrderedLocusNames=TEPIRE1_2369 {ECO:0000313|EMBL:CCP27211.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP27211.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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DR EMBL; HF563609; CCP27211.1; -; Genomic_DNA.
DR RefSeq; WP_013779242.1; NC_019954.2.
DR AlphaFoldDB; F4LRY4; -.
DR STRING; 1209989.TepRe1_2201; -.
DR KEGG; tae:TepiRe1_2369; -.
DR KEGG; tep:TepRe1_2201; -.
DR PATRIC; fig|1209989.3.peg.2726; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_002569_5_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000010802; 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:CCP27211.1};
KW Pyruvate {ECO:0000313|EMBL:CCP27211.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 16..239
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 262..366
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 393 AA; 43023 MW; FED723523F99EF29 CRC64;
MKNKVALTGN EAVAQAMRQI NPDVVAAYPI TPSTEVVQMF SSFVANGKVD TEFVTVESEH
SAMSATMGAS AAGARAMTCT SSQGLAYMFE VVYVAASMRL PIVFPVANRA LSGPINIHCD
HSDAMGIKQA GVIQLFSENA QEAYDNMIQA IRIAEHPDVQ LPVSVNYDGF ITSHALDVLE
ILDDETVRNF IGVYKPHEAL LNVNKPVSMG NFDMYDYYFE HKYQQVAAME AAKRVIEEVG
KEYAKISGRN YGLVDAYKLD DADMAVVVMN SAAGSSKGVC DELRAKGLKV GVLKPRAFRP
FPHEAIADAL KGVKAVAVLD RAETFSTLGG PMFADVRNSL YDLKNDIKVV NYVYGLGGRD
LRLEDVEQIY SDLDDIIKTG KVDNFVRYLG LRE
//
