OFOB2_SULTO
ID OFOB2_SULTO Reviewed; 304 AA.
AC Q96XT4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 2, subunit beta {ECO:0000303|PubMed:27619895};
DE Short=OFOR2 {ECO:0000303|PubMed:27619895};
DE EC=1.2.7.11 {ECO:0000269|PubMed:27619895};
GN Name=ST2433 {ECO:0000312|EMBL:BAB67543.1};
GN OrderedLocusNames=STK_24330 {ECO:0000312|EMBL:BAB67543.1};
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 IRON-SULFUR
RP (4FE-4S); MAGNESIUM ION AND THIAMINE PYROPHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:27619895};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:27619895};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:27619895};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:27619895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27619895};
CC Note=Binds 1 Mg(2+) per subunit. {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}.
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DR EMBL; BA000023; BAB67543.1; -; Genomic_DNA.
DR RefSeq; WP_010980518.1; NC_003106.2.
DR PDB; 5B46; X-ray; 2.10 A; B=1-304.
DR PDB; 5B47; X-ray; 2.20 A; B=1-304.
DR PDBsum; 5B46; -.
DR PDBsum; 5B47; -.
DR AlphaFoldDB; Q96XT4; -.
DR SMR; Q96XT4; -.
DR STRING; 273063.STK_24330; -.
DR EnsemblBacteria; BAB67543; BAB67543; STK_24330.
DR GeneID; 1460516; -.
DR KEGG; sto:STK_24330; -.
DR PATRIC; fig|273063.9.peg.2751; -.
DR eggNOG; arCOG01599; Archaea.
DR OrthoDB; 43666at2157; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019164; F:pyruvate synthase activity; IDA:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:UniProtKB.
DR InterPro; IPR011896; OFOB.
DR InterPro; IPR032686; PFO_beta_C.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF12367; PFO_beta_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR02177; PorB_KorB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..304
FT /note="2-oxoacid:ferredoxin oxidoreductase 2, subunit beta"
FT /id="PRO_0000445534"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 44..47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000305|PubMed:27619895"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 91..92
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT BINDING 122..123
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47"
FT SITE 125
FT /note="Plays an important role in the binding of CoA"
FT /evidence="ECO:0000250|UniProtKB:Q96Y68"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:5B46"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:5B46"
FT TURN 273..277
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5B46"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:5B46"
SQ SEQUENCE 304 AA; 33809 MW; 3A0245B9BB9E7EF7 CRC64;
MVERKPVFVD WCPGCGDFGI LRAEEMAIRE LGINPKSVVI VSGIGCSGKI PHFMNLPISG
VHTLHGRSIA FATGIKLSNP SLEVIVNVGD GDGLGIGMGH FVHLGRRNID IAVLVHNNGV
YGLTKGQASP TLHRGEKTKS LPKPNIMDAV NPLAVALAAG YTFVARGYAY DVMHLKELIK
KAILHKGSAL VDILQPCPTY NDINTKEWYD KRVYKLDNVP GWDPVVRKEE EAQKKFEQAI
MKSYEWGEKI PIGIFYQNEL VPTFEDRLTS NIPNYREYYP AKQQIEINGI STTKIDELIK
AKRI
