位置:首页 > 蛋白库 > OFOA2_AERPE
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024