OFOA_SACSO
ID OFOA_SACSO Reviewed; 632 AA.
AC A0A0E3JT70;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase subunit alpha {ECO:0000303|PubMed:16466637};
DE Short=OFOR {ECO:0000305};
DE EC=1.2.7.11 {ECO:0000269|PubMed:16466637};
GN ORFNames=SSOP1_2913 {ECO:0000312|EMBL:SAI86467.1},
GN SULA_0623 {ECO:0000312|EMBL:AKA78407.1},
GN SULB_0625 {ECO:0000312|EMBL:AKA73017.1},
GN SULC_0623 {ECO:0000312|EMBL:AKA75715.1};
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98/2 SULC {ECO:0000312|EMBL:AKA75715.1,
RC ECO:0000312|Proteomes:UP000033057}, SULA {ECO:0000312|EMBL:AKA78407.1,
RC ECO:0000312|Proteomes:UP000033106}, and
RC SULB {ECO:0000312|EMBL:AKA73017.1, ECO:0000312|Proteomes:UP000033085};
RX PubMed=26021927; DOI=10.1128/genomea.00549-15;
RA McCarthy S., Gradnigo J., Johnson T., Payne S., Lipzen A., Martin J.,
RA Schackwitz W., Moriyama E., Blum P.;
RT "Complete Genome Sequence of Sulfolobus solfataricus Strain 98/2 and
RT Evolved Derivatives.";
RL Genome Announc. 3:E00549-E00549(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1
RC {ECO:0000312|EMBL:SAI86467.1};
RA Shah S.A., Garrett R.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=16466637; DOI=10.5483/bmbrep.2006.39.1.046;
RA Park Y.J., Yoo C.B., Choi S.Y., Lee H.B.;
RT "Purifications and characterizations of a ferredoxin and its related 2-
RT oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon,
RT Sulfolobus solfataricus P1.";
RL J. Biochem. Mol. Biol. 39:46-54(2006).
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:0000269|PubMed:16466637}.
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:0000269|PubMed:16466637};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=163 uM for 2-oxoglutarate {ECO:0000269|PubMed:16466637};
CC KM=275 uM for pyruvate {ECO:0000269|PubMed:16466637};
CC KM=516 uM for 2-oxobutyrate {ECO:0000269|PubMed:16466637};
CC Note=kcat is 452 min(-1) for 2-oxoglutarate as substrate. kcat is 144
CC min(-1) for pyruvate as substrate. kcat is 93 min(-1) for 2-
CC oxobutyrate as substrate.;
CC pH dependence:
CC Optimum pH is between 7-8. {ECO:0000269|PubMed:16466637};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:16466637};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:16466637}.
CC -!- DOMAIN: The Tyr-Pro-Ile-Thr-Pro (YPITP) motif is important for the
CC turnover of the reaction, presumably through its flexibility and
CC mobility. {ECO:0000250|UniProtKB:P72578}.
CC -!- MASS SPECTROMETRY: Mass=69300; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16466637};
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DR EMBL; CP011055; AKA73017.1; -; Genomic_DNA.
DR EMBL; CP011056; AKA75715.1; -; Genomic_DNA.
DR EMBL; CP011057; AKA78407.1; -; Genomic_DNA.
DR EMBL; LT549890; SAI86467.1; -; Genomic_DNA.
DR RefSeq; WP_009989033.1; NZ_LT549890.1.
DR AlphaFoldDB; A0A0E3JT70; -.
DR SMR; A0A0E3JT70; -.
DR EnsemblBacteria; AKA73017; AKA73017; SULB_0625.
DR EnsemblBacteria; AKA75715; AKA75715; SULC_0623.
DR EnsemblBacteria; AKA78407; AKA78407; SULA_0623.
DR GeneID; 44128564; -.
DR KEGG; ssoa:SULA_0623; -.
DR KEGG; ssof:SULC_0623; -.
DR KEGG; ssol:SULB_0625; -.
DR PATRIC; fig|2287.6.peg.649; -.
DR OrthoDB; 41678at2157; -.
DR Proteomes; UP000033057; Chromosome.
DR Proteomes; UP000033085; Chromosome.
DR Proteomes; UP000033106; Chromosome.
DR Proteomes; UP000076770; Chromosome i.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IDA:UniProtKB.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IDA:UniProtKB.
DR GO; GO:0019164; F:pyruvate synthase activity; IDA:UniProtKB.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.920.10; -; 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 Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR SUPFAM; SSF53323; SSF53323; 1.
DR TIGRFAMs; TIGR03710; OAFO_sf; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Pyruvate.
FT CHAIN 1..632
FT /note="2-oxoacid:ferredoxin oxidoreductase subunit alpha"
FT /id="PRO_0000445527"
FT MOTIF 254..258
FT /note="YPITP motif"
FT /evidence="ECO:0000250|UniProtKB:P72578"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
SQ SEQUENCE 632 AA; 70228 MW; 6648EF7531835277 CRC64;
MRISWMIGGA QGSGVDTSAN IFGNAVAASG YYIYGNREYY SNIKGRHSYF NLTISDKPPR
SIAQQIEILT SFDAETIFQH FNEVKDVLIY STEVENTKAE QVQSMEPEIT EHVVKFLKEK
GYGTTVKDVI NYLKKEKGVK VIPIDYMEIL KKVADQAKVQ LSVADRARNT IAIAASYKLL
GLKEQYLINS ITRTFRQEVF AKINTIAAQL AMQQIQPMYN LPELPNNEEK INLDGNTAAA
IGKIYGGLRF QSYYPITPAS DESVFIEAHQ TVFTVDPKTG EKRKSTIVVV QAEDELAAIN
MASGAALTGV RAATATSGPG FSLMVEGMGW AGMNEVPVVI TYYIRGGPST GQPTRTSQAD
LMFALNAGHG EFPRIVIASG DHVEAFHDGT WALNLAQKYQ TPVIHLVDKA LANSYSIIPK
KTLGMENIRI EKGKIVINTN TPELKRFEIT EDGISPFAPL GTARVHYTGD EHDEYGFIAE
ASENREKMYE KRIKKLMTAD KEIPEESRVN VYGNTDSKVA IITWGSPKGA ILDAMEELEN
EGIKPMLIQI RMFSPFPKNL MRKLLNGKEF IIDVESNYFG QAGEVLKLNT GIEPTHYILK
WNGRPMMRDE VKEGIKAVVQ KGERRVVLHG GA
