ID A8F4Q2_PSELT Unreviewed; 564 AA.
AC A8F4Q2;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ABV33136.1};
GN OrderedLocusNames=Tlet_0570 {ECO:0000313|EMBL:ABV33136.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33136.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV33136.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV33136.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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DR EMBL; CP000812; ABV33136.1; -; Genomic_DNA.
DR RefSeq; WP_012002617.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F4Q2; -.
DR STRING; 416591.Tlet_0570; -.
DR KEGG; tle:Tlet_0570; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_0; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000002016; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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 Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:ABV33136.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002016}.
FT DOMAIN 11..172
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 207..439
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 564 AA; 62629 MW; B46F2CA4BB35BBAF CRC64;
MEYSFIIAGE AGQGIQTVEV LLPKIFKKAG LNVFSYKEYM SRVRGGSNST LIRVSDIPVR
AFKQKADFAL FLSNDVSHLK RISNRLSSDS ILVVDEEFPG IDDTLKVLRI PLLKTASALG
NKIYANSVMI GFATALLGVD LENTLNIVKQ YFSKKSKEVI FQNLEAVKSG YENGLASKKK
LSITKLKQNK QICDQFLLSG AEAVAFGALA GGCNFISSYP MSPSTGVLVQ LAKLSDNFDL
IVEQTEDEIS AINMALGAWY AGGRAMVTTS GGGFALMIEG LSLAGMIESP IVVHLAQRPG
PATGLPTRTE QADLMFALYA GHGEFPRVIY APGNLEEAFL CSWKAFQIAD KYQIPALILT
DQYLMDMIYN IENVPLPENI ENYLIKTDSD YLRYKLTQKG ISPRGIPGWG EGLVCVDSDE
HDESGRITED FEMRKMMVEK RMKKMSNFKD YYTPELTGNS GYEVLAVCFG STKEIVKEAA
QSFENIAVLH LVQLYPLPRD LKKYFDMAKK VVIIENNFTS QFASLLKTFA NLDHSKKVTK
YDGMPFSVEE IKNVFEQFTE EGEV
//
