OFOA2_AERPE
ID OFOA2_AERPE Reviewed; 642 AA.
AC Q9YBX7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha {ECO:0000303|PubMed:15848165};
DE Short=OFOR2 {ECO:0000303|PubMed:15848165};
DE EC=1.2.7.11 {ECO:0000269|PubMed:15848165};
GN OrderedLocusNames=APE_1473.1 {ECO:0000312|EMBL:BAA80471.2};
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, glyoxylate and
CC 2-oxoglutarate to form their CoA derivatives.
CC {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=380 uM for pyruvate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15848165};
CC KM=500 uM for 2-oxoglutarate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15848165};
CC Vmax=8 umol/min/mg enzyme with pyruvate as substrate (at 80 degrees
CC Celsius) {ECO:0000269|PubMed:15848165};
CC Vmax=7.46 umol/min/mg enzyme with 2-oxoglutarate as substrate (at 80
CC degrees Celsius) {ECO:0000269|PubMed:15848165};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:15848165};
CC Temperature dependence:
CC Optimum temperature is over 110 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; BAA80471.2; -; Genomic_DNA.
DR PIR; A72627; A72627.
DR AlphaFoldDB; Q9YBX7; -.
DR SMR; Q9YBX7; -.
DR STRING; 272557.APE_1473.1; -.
DR EnsemblBacteria; BAA80471; BAA80471; APE_1473.1.
DR KEGG; ape:APE_1473.1; -.
DR PATRIC; fig|272557.25.peg.998; -.
DR eggNOG; arCOG01606; Archaea.
DR OMA; EFWSNIA; -.
DR Proteomes; UP000002518; Chromosome.
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; Reference proteome.
FT CHAIN 1..642
FT /note="2-oxoacid:ferredoxin oxidoreductase 2, subunit
FT alpha"
FT /id="PRO_0000445537"
FT MOTIF 263..267
FT /note="YPITP motif"
FT /evidence="ECO:0000250|UniProtKB:P72578"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
SQ SEQUENCE 642 AA; 69900 MW; 3A88CB94FC16852C CRC64;
MVDISLIIGG PQGGGIESAG QIAIKSMVLL GYEVLGSREY HSNIMGAHSY YHLRVQQHRP
RSLKLPVDGV LALDAESVFT HFRDVRPGGI LVYDPGTKST RVDAIQPMAG PLKKRLKSLF
DSRGMQPVVE SAVKLAEEAG ARIVGLPLKE MLKTLSERTG APVARVSRAL NTLGLASMLY
MLGVPVEYIE KAISLQFAGK EKVINMNVEA VRIAVDYVRE AFGEPESRLP PGPRRGQTMM
VATGNDLVAM GKIVGGLGVI TYYPITPSSD EALYVEKHSY ISIDGPLAEK LGYDKIAVAI
VQMEDELASI NAVLGAAAAG ARASTTTSGP GFSLMNEAVS LAVEAEIPVV VTLWMRAGPS
TGMPTRTGQQ DLLHSIFSGH GDAPKIVLAS GDHVEAFYDA IKAFNWAEEF QTPVIHLLDK
YLASSMVSLA REDLDPSKVP ITRGKLLDNP PADYRRYEVV EDGISPRARL GSATMVITGL
EHDEYGYATE DPVMREIMMF KRERKFKVIE ERIPDEEKAV LHGDSEASVA LVSFGSTKQP
ILEALEMLRD EGVRARFAQV RLLYPFPGRL VEEMLEGVEK VIMVEQNLLG QLAMLLRAHT
SIKPDSSIVK INGRPLYSFE VAGAVKRILE TGEERVVVSH GS