ID A0A101XEY9_9CREN Unreviewed; 643 AA.
AC A0A101XEY9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=AT713_00220 {ECO:0000313|EMBL:KUO90129.1};
OS Caldivirga sp. JCHS_4.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=1714254 {ECO:0000313|EMBL:KUO90129.1, ECO:0000313|Proteomes:UP000055041};
RN [1] {ECO:0000313|EMBL:KUO90129.1, ECO:0000313|Proteomes:UP000055041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342; EC=1.2.7.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000005};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO90129.1}.
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DR EMBL; LOCD01000164; KUO90129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101XEY9; -.
DR Proteomes; UP000055041; Unassembled WGS sequence.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
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; IPR033412; PFOR_II.
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 NCBIfam; NF041170; Oxoac_fdxalpha_Archa; 1.
DR PANTHER; PTHR32154:SF16; PYRUVATE FLAVODOXIN_FERREDOXIN OXIDOREDUCTASE DOMAIN PROTEIN; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 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:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:KUO90129.1}.
FT DOMAIN 14..219
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 252..501
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 528..614
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 643 AA; 71789 MW; D6AC8C5F63A1F55F CRC64;
MPVDLMWVIG GPQGGGIDTG ANVFMRAVAR AGYYVIGDRE YFSNIKGRHS YFMVRVSDEP
RGGLLSPIDV LVALDAETVF THFQDVKRGG YVVVDTSTFN TRLDQLQYME DELKDRLREW
FSRAGVEPTV KGIVDYLRSN GVNVMIMHYA DLLQEVKKKL HDVDLPSLIG RYSNVVMTAY
STAAMGLPME YVFKGLEDVF TGRRGKLLEY NKAIVEVVYE YAKPMKTNIT LSPIKRGVRA
IIVNGNEAVA MGKILGGLRF QTYYPITPAA DESFFIEAHD TVDLDPVTEE AKALEKAGIV
VVQTEDEISA INMAIGAGIA GARSATATSG PGLSLMVEGV GFAGMNEVPV VITHYQRSGP
STGMATRNSQ SDLRFVMHMG HGEFPRIVIS SGDHREAIED AFKALNWAER YQMPVFHLVD
KALANSYSTV IWDLDKKSLK IDRGLIVTKD ENNYRRFRIT KDGVSPRSIP GLGPIFWLTG
DEHDEYGHIT EDPVTRTEMY EKRMKKLELA DKEIPLEDKA RLYGPEDADV TIVGWGSTKG
AIIDAMNVLN NEGYKVNFLQ LRMFIPFPTE FVRRVLGRGQ LIIDVESNYE SQAASVIRER
TGIEIKHRVV KVTGRPIFVD EVYEAVKKIL KDGDEEIVLM KGP
//
