OFOA1_AERPE
ID OFOA1_AERPE Reviewed; 639 AA.
AC Q9YA13;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha {ECO:0000303|PubMed:15848165};
DE Short=OFOR1 {ECO:0000303|PubMed:15848165};
DE EC=1.2.7.11 {ECO:0000269|PubMed:15848165};
GN OrderedLocusNames=APE_2126.1 {ECO:0000312|EMBL:BAA81137.2};
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1
RC {ECO:0000312|Proteomes:UP000002518};
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=15848165; DOI=10.1016/j.febslet.2004.11.117;
RA Nishizawa Y., Yabuki T., Fukuda E., Wakagi T.;
RT "Gene expression and characterization of two 2-oxoacid:ferredoxin
RT oxidoreductases from Aeropyrum pernix K1.";
RL FEBS Lett. 579:2319-2322(2005).
CC -!- FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation
CC of different 2-oxoacids such as pyruvate, 2-oxobutyrate and glyoxylate
CC to form their CoA derivatives. {ECO:0000269|PubMed:15848165}.
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:15848165};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=240 uM for pyruvate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15848165};
CC Vmax=10.1 umol/min/mg enzyme with pyruvate as substrate (at 80
CC degrees Celsius) {ECO:0000269|PubMed:15848165};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:15848165};
CC Temperature dependence:
CC Optimum temperature is 105 degrees Celsius.
CC {ECO:0000269|PubMed:15848165};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:15848165}.
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}.
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DR EMBL; BA000002; BAA81137.2; -; Genomic_DNA.
DR PIR; A72519; A72519.
DR AlphaFoldDB; Q9YA13; -.
DR SMR; Q9YA13; -.
DR STRING; 272557.APE_2126.1; -.
DR EnsemblBacteria; BAA81137; BAA81137; APE_2126.1.
DR KEGG; ape:APE_2126.1; -.
DR PATRIC; fig|272557.25.peg.1416; -.
DR eggNOG; arCOG01606; Archaea.
DR OMA; YYQRGGP; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate 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; Reference proteome.
FT CHAIN 1..639
FT /note="2-oxoacid:ferredoxin oxidoreductase 1, subunit
FT alpha"
FT /id="PRO_0000445535"
FT MOTIF 266..270
FT /note="YPITP motif"
FT /evidence="ECO:0000250|UniProtKB:P72578"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
SQ SEQUENCE 639 AA; 71081 MW; F5C799AC79F6F154 CRC64;
MRKDVVLLVG GAQGSGLETT MQVLAPAYAS LGYGVLANRE YFSNIVGRHS YIHIRVSSSG
EARPLYYPAD FLGAMDAETV FTHWDDIGEG AFLLYDLGTA RMRLQQIASM EPDLRSRLMQ
QYREAGIEPF TVEKVVEYLE REKRVRVIGL SFTALFDVLI KKHGLSRAQA QRFRSSILIG
AIAGLTSLDR EALDLGLQRR FGSRPKVLEI NRDFIASVAD EVEKEYGAQL KLEPAEPKSG
EYVVASGNDV VAMGKVVGGV RYQAYYPITP ASDESVLLEE FEGLKIDGES LGSIAILQTE
DEIAAVSSVI GAALTGARAS TATSGPGFSL MVEALGWAGK NDVPMVITYY QRGGPSTGLP
TRGSQSDLLF SLFASHGEFP RIILSSGDHL EAFYDAIEAY NLAERFQMPV IHLLDKFLAN
MVASVPFPDW KAIKIDRGKT LFKAPTGPFK RFPRDQPLAD RPVLGSGAIT WYTGDENDEY
GHIDEDPVNR LVMYERRWKK MEIADREIPE DFRVKYYGDE DAEVLLVGWG SVKIPALEAI
ERLREMGVNA AYLHLRMLSP LPKRRVSEVL SRFDADRVIA VEANYLGQAS KIVTMETGFM
FRKYILKWTG RPVYLHELVE GVLDIVRNGR DKVVLSYGK
