OFOA1_SULTO
ID OFOA1_SULTO Reviewed; 627 AA.
AC Q96Y66;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha {ECO:0000303|PubMed:27619895};
DE Short=OFOR1 {ECO:0000303|PubMed:27619895};
DE EC=1.2.7.11 {ECO:0000269|PubMed:27619895, ECO:0000305|PubMed:19027887};
GN Name=ST2300 {ECO:0000312|EMBL:BAB67411.1};
GN OrderedLocusNames=STK_23000 {ECO:0000312|EMBL:BAB67411.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7
RC {ECO:0000312|Proteomes:UP000001015};
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=19027887; DOI=10.1016/j.bbapap.2008.10.006;
RA Luo J., Fukuda E., Takase H., Fushinobu S., Shoun H., Wakagi T.;
RT "Identification of the lysine residue responsible for coenzyme A binding in
RT the heterodimeric 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus
RT tokodaii, a thermoacidophilic archaeon, using 4-fluoro-7-nitrobenzofurazan
RT as an affinity label.";
RL Biochim. Biophys. Acta 1794:335-340(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-41; THR-349 AND ASP-468,
RP AND SUBUNIT.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=27619895; DOI=10.1038/srep33061;
RA Yan Z., Maruyama A., Arakawa T., Fushinobu S., Wakagi T.;
RT "Crystal structures of archaeal 2-oxoacid:ferredoxin oxidoreductases from
RT Sulfolobus tokodaii.";
RL Sci. Rep. 6:33061-33061(2016).
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:0000269|PubMed:19027887, ECO:0000269|PubMed:27619895}.
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:27619895, ECO:0000305|PubMed:19027887};
CC -!- ACTIVITY REGULATION: Inhibited by low concentration of 4-fluoro-7-
CC nitrobenzofurazan (NBD-F). {ECO:0000269|PubMed:19027887}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for pyruvate {ECO:0000269|PubMed:27619895};
CC KM=2.1 mM for 2-oxoglutarate {ECO:0000269|PubMed:27619895};
CC Vmax=7.5 umol/min/mg enzyme with pyruvate as substrate
CC {ECO:0000269|PubMed:27619895};
CC Vmax=2.7 umol/min/mg enzyme with 2-oxoglutarate as substrate
CC {ECO:0000269|PubMed:27619895};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:27619895}.
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; BA000023; BAB67411.1; -; Genomic_DNA.
DR RefSeq; WP_010980386.1; NC_003106.2.
DR PDB; 5B48; X-ray; 2.50 A; A/C=1-627.
DR PDBsum; 5B48; -.
DR AlphaFoldDB; Q96Y66; -.
DR SMR; Q96Y66; -.
DR STRING; 273063.STK_23000; -.
DR EnsemblBacteria; BAB67411; BAB67411; STK_23000.
DR GeneID; 1460384; -.
DR KEGG; sto:STK_23000; -.
DR PATRIC; fig|273063.9.peg.2606; -.
DR eggNOG; arCOG01606; Archaea.
DR OMA; AGYYIYG; -.
DR OrthoDB; 41678at2157; -.
DR BRENDA; 1.2.7.11; 15396.
DR Proteomes; UP000001015; 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; 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; 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 3D-structure; Oxidoreductase; Pyruvate; Reference proteome.
FT CHAIN 1..627
FT /note="2-oxoacid:ferredoxin oxidoreductase 1, subunit
FT alpha"
FT /id="PRO_0000445531"
FT MOTIF 253..257
FT /note="YPITP motif"
FT /evidence="ECO:0000250|UniProtKB:P72578"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96XT2"
FT MUTAGEN 41
FT /note="S->A: Same oxidoreductase activity as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:27619895"
FT MUTAGEN 349
FT /note="T->L: Same oxidoreductase activity as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:27619895"
FT MUTAGEN 468
FT /note="D->A: Loss of oxidoreductase activity toward 2-
FT oxoglutarate but retains its activity toward pyruvate."
FT /evidence="ECO:0000269|PubMed:27619895"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 43..57
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 480..500
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 576..585
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 603..614
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:5B48"
SQ SEQUENCE 627 AA; 70246 MW; A0A2046F12232590 CRC64;
MRLSWVIGGA QGTGIDTAAN IFGNAVASAG YYIYGNREYY SNIKGRHSYF SLTISDKRVR
SNTQKIDILV SFDAETVFQH FYDVKDILIY NKAVETTKID AVQSMEPELA ERIKDFLTKQ
GYETTVKGAL EYASKNNVTL IPVNYDEIAK KVADEMKVPL SVTERVKNIV GITISYKLLG
LDVNYLIEAI NSTFKQDLYR KMNELAVKDS YDIVESRYNL KPSSKERRRF WLDGNTAVAI
GKIYGGVRFQ SYYPITPASD ESVYIEAHQD VLMEDPITGD KKKGTIVVVQ AEDELAAINM
AIGAALTGVR AATATSGPGF SLMVEGLGWA GMNEVPVVIT YYIRGGPSTG LPTRTAQSDL
IFPIFAGHGE FPKIVLASGD HAEAFKDAIW ALNLAEKYQT PVIHLVEKTL ANSYSTIPYE
ELELDKLKAE RGKIVESGDI SYKRFKFTED GISPRAFLGK ATMYYTGDEH NEEGHISEDV
VNRTMMYEKR MKKLEVADKE IPEESRVKIY GDLNSRNLII TWGSPTGVLR DILEESNFDF
TLLQIRMFSP FPKNLVSKLM EGRDKIITVE GNYLAQTSLL VKMYTGKDVT NSILKWNGRP
FLRDELEEAL IKVIKDGEKR VVLNGGI
