ID D9Q308_ACIS3 Unreviewed; 638 AA.
AC D9Q308;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=ASAC_1291 {ECO:0000313|EMBL:ADL19696.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19696.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19696.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
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}.
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DR EMBL; CP001742; ADL19696.1; -; Genomic_DNA.
DR RefSeq; WP_013267208.1; NC_014374.1.
DR AlphaFoldDB; D9Q308; -.
DR STRING; 666510.ASAC_1291; -.
DR GeneID; 9499546; -.
DR KEGG; asc:ASAC_1291; -.
DR eggNOG; arCOG01606; Archaea.
DR HOGENOM; CLU_017038_1_0_2; -.
DR InParanoid; D9Q308; -.
DR OrthoDB; 31112at2157; -.
DR Proteomes; UP000000346; Chromosome.
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 ECO:0000313|EMBL:ADL19696.1}; Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT DOMAIN 15..217
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 254..493
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 521..609
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 638 AA; 69962 MW; EF443F9242965F96 CRC64;
MALKEVHLLL GGPQGAGVET SASVLTASLA GLGYGIMSDR EYYSNIVGRH SYVHFTISAT
SFPRSLTYPV ELVGAMDAES VLTHFHEVAP GGVLVYDAGV DKTKISQVIS MEPEVRERVE
ARFKEYGLEP TVGNAAKIVE EKLNAHSVPL DFRKILDEAR QKLGVSSVEV QRYRNSILLG
AAAAVLGVDP EVIRDGLSVR FKGNQKIVNA NMVVIGLTME SVPKDVRGLA KLDEPKLDVE
EMISASGNDV IGMAKIVGGV RYQSYYPITP ASDESVFIEA HQAVSVDGKP VGSIVVFQTE
DELAAINSAI GAALTGVRAA TATSGPGFSL MAEGLGWAGH NEVPLLITFY QRGGPSTGQP
TRGEQADLLF SLFASHGEFP RIVIASGDIE EAFYDTLKAL NWAERFQVPV IHLVDKYMAN
VISAMRMPDP SKVKVDRGKL ILKASGPMKR FDLSDPISPR PAIGSGAITW YTGDEHNEWG
HISEDPINRV KMYDKRMKKL EIMDQEIPVE ERAVYYGDDN ADFLLVGWGF VKGAALDALE
ELKQEGYHGA YLHLKVFSPF PSKYVADILS KFDPKRVIDV EHNYLGQAAK VIEMNTGFEI
SRFILKYTGR PMYRMELKEA VKRILEGKSV REVLTYGE
//
