ID C3N9Y3_SULIY Unreviewed; 385 AA.
AC C3N9Y3;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=YG5714_0374 {ECO:0000313|EMBL:ACP44667.1};
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386 {ECO:0000313|EMBL:ACP44667.1, ECO:0000313|Proteomes:UP000002308};
RN [1] {ECO:0000313|EMBL:ACP44667.1, ECO:0000313|Proteomes:UP000002308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #1 {ECO:0000313|Proteomes:UP000002308};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001403; ACP44667.1; -; Genomic_DNA.
DR RefSeq; WP_012712963.1; NC_012622.1.
DR AlphaFoldDB; C3N9Y3; -.
DR GeneID; 8760221; -.
DR KEGG; siy:YG5714_0374; -.
DR HOGENOM; CLU_002569_5_0_2; -.
DR Proteomes; UP000002308; Chromosome.
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 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:SF30; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR32154; 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 Pyruvate {ECO:0000313|EMBL:ACP44667.1}.
FT DOMAIN 20..242
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 265..365
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 385 AA; 43492 MW; 53F3998AC97DC7AC CRC64;
MQVLKRKTLA LVGNHAVAYA VKQSKPQVLA VFPITPQTTM LEKISEYIAS EELNAELIKV
ESEHSALASI YGAALAGARV FTATSSQGLL YMTEMIYWAG GQRVPMVAAV ATRAIAEPWS
IWDDHQDFLS KRDAIWIQMM AENVQEAYDM TIQAFRISED ERVILPVMMG FDGFILTHTM
ERIEVLEDGE VDNFLPPRQF NLIDFSDPIG VGPIATPEDY IKYRYEAMKA MERAKGVIEE
VMNEYERISG RKQNGLVECY KCEDAKYVFV TMGAWSGDCK VAVDRLRDAG VEAGLLKIRV
FRPFPKEKIE EYLRSMKGVI VLDRAYSYGS GGILANEIKA TLYGYRVPVY SVIAGIGGKD
VRPRHFQKVI EDLINDNLEE ERWLL
//
