OFOA2_SULTO
ID OFOA2_SULTO Reviewed; 628 AA.
AC Q96XT2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha {ECO:0000303|PubMed:27619895};
DE Short=OFOR2 {ECO:0000303|PubMed:27619895};
DE EC=1.2.7.11 {ECO:0000269|PubMed:27619895};
GN Name=ST2435 {ECO:0000312|EMBL:BAB67545.1};
GN OrderedLocusNames=STK_24350 {ECO:0000312|EMBL:BAB67545.1};
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 X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
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: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};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for pyruvate {ECO:0000269|PubMed:27619895};
CC KM=15 mM for 2-oxoglutarate {ECO:0000269|PubMed:27619895};
CC Vmax=7 umol/min/mg enzyme with pyruvate as substrate
CC {ECO:0000269|PubMed:27619895};
CC Vmax=1.4 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; BAB67545.1; -; Genomic_DNA.
DR PDB; 5B46; X-ray; 2.10 A; A=1-628.
DR PDB; 5B47; X-ray; 2.20 A; A=1-628.
DR PDBsum; 5B46; -.
DR PDBsum; 5B47; -.
DR AlphaFoldDB; Q96XT2; -.
DR SMR; Q96XT2; -.
DR STRING; 273063.STK_24350; -.
DR EnsemblBacteria; BAB67545; BAB67545; STK_24350.
DR KEGG; sto:STK_24350; -.
DR PATRIC; fig|273063.9.peg.2752; -.
DR eggNOG; arCOG01606; Archaea.
DR OMA; TPVIHII; -.
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; 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 3D-structure; Oxidoreductase; Pyruvate; Reference proteome.
FT CHAIN 1..628
FT /note="2-oxoacid:ferredoxin oxidoreductase 2, subunit
FT alpha"
FT /id="PRO_0000445533"
FT MOTIF 254..258
FT /note="YPITP motif"
FT /evidence="ECO:0000250|UniProtKB:P72578"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B47"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B47"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 44..58
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 480..500
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 524..535
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 554..561
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 565..575
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 604..617
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:5B46"
SQ SEQUENCE 628 AA; 70218 MW; F356B1F46FD4E523 CRC64;
MTRIVWMIGG AQGLGVDTSA NIFGNAVAKA GYYLFGNREY YSNIKGRHSY FEVVISEKPI
RSLSSYVNIL ASFDAETVFQ HFTETKEYLI YNVEYENTTV DLVKSMEPEM AEQVKEALSK
ERLGFTIKDV LEYLKRRGVK VIGFNYTELI KKIADTFKVP MSVVERAKNM IAVGASYGLL
GLKFDYLKDA ISSTFKNELF IKFNTMAAEL GYNSVPNVYK LQEYKIEKQR IQVDGNTISA
MGKLAGGLRF QSYYPITPAS DESVYIEANQ NLDMIVEGNE LRKGGVVVVQ AEDELAAINM
AVGAALTGVR SATATSGPGF SLMSEGISWA GMNEVPVVIT YYMRGAPATG LPTRSGQADL
KFALNVGHGE FPRIVIASGD HVEIFWDAIW ALNLAEKYQT PVIHIIEKTL ANAYSVFEEE
LITNRPYVIE RGKIVKPTSD YFNRFEVTED GISPRVFLGQ ASIFYTGDEH NEEGHITENS
INRMKMYEKR NKKLETADKE IPEEQRVNIV GDADIVLLTW GSPKGAILDA MEELSKDGIK
TMMVQVKMFN PYPKNLMKKI LSGKSKIIAV ENNYNAQGAE VLAEKTGIFA TNYILKWTGR
PITREEVIEG IKKILERDEK RVVLYGGA
