ID A0A031LPY7_9CREN Unreviewed; 623 AA.
AC A0A031LPY7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN ORFNames=CM19_07815 {ECO:0000313|EMBL:EZQ04878.1};
OS Candidatus Acidianus copahuensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=1160895 {ECO:0000313|EMBL:EZQ04878.1, ECO:0000313|Proteomes:UP000024332};
RN [1] {ECO:0000313|EMBL:EZQ04878.1, ECO:0000313|Proteomes:UP000024332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALE1 {ECO:0000313|EMBL:EZQ04878.1,
RC ECO:0000313|Proteomes:UP000024332};
RA Urbieta M.S., Rascovan N., Castro C., Revale S., Giaveno M.A.,
RA Vazquez M.P., Donati E.R.;
RT "Draft genome sequence of the novel thermoacidophilic archaea Acidianus
RT copahuensis ALE1 strain, isolated from Copahue volcanic area in Neuquen
RT Argentina.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation
CC of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-
CC oxobutyrate to form their CoA derivatives.
CC {ECO:0000256|ARBA:ARBA00003908}.
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:EZQ04878.1}.
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DR EMBL; JFZT01000044; EZQ04878.1; -; Genomic_DNA.
DR RefSeq; WP_048099799.1; NZ_JFZT01000044.1.
DR AlphaFoldDB; A0A031LPY7; -.
DR STRING; 1160895.CM19_07815; -.
DR OrthoDB; 31112at2157; -.
DR Proteomes; UP000024332; Unassembled WGS sequence.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0047553; F:2-oxoglutarate 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000024332}.
FT DOMAIN 12..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 241..485
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 512..603
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 623 AA; 68697 MW; 100AC0A6A487A04D CRC64;
MRYSWMIGGA QGLGVDTSAV IFGNSISKAG YYIFGNREYY SNIKGRHSYF QVVFSEKPVH
SISSKVDVLA TFDAETIFQH FTEVKDVMIY DDSLKNVTVD MVRSIEPEIA EGVKEELKKN
AFGFSVGDVV KYVESKGVKT IPVDYSSILK KVADTYHIPL SVVERAKNIV VVAISLSLFG
IKEEHLRNAI ASEFKNDLFV KFNTTAAEIG YSLVQAKYNL PELNVGEPRI QVDGNTISAI
GKLSAGLRFQ SYYPITPASD ESTYIEANQN LDLIVNGERR KGGAVVVQAE DELAAINMAV
GSALTGTRSA TATSGPGFSL MAEGISWAGM NEVPVVITYY MRGAPSTGLP TRSGQGDLKF
ALNVGHGEFP RIVIASGDHK EIYWDAIWAF NLAEKYQTPV IHVIEKTLAN AYSSFDEKEL
DGNVEVERGK IVKPEGGYFN RFEFSEDGIS PRAFLGDAGI FHAGDEHNEE GHITEGTKNR
ILMYEKRMKK LYTADREIPE VQRVNVVGDG QVVLLTWGSP KGSILDAMPL LQNEGVKVQM
VQVRMFNPYP SDLMKKLLSG KKVIAIENNY CAQGAQVLSE RTGIFPDSFI LKWTGRSITM
EEIIEGVKKV MQGEKRVVLS DGA
//
