OFOB1_SULTO
ID OFOB1_SULTO Reviewed; 305 AA.
AC Q96Y68;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 1, subunit beta {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=ST2298 {ECO:0000312|EMBL:BAB67409.1};
GN OrderedLocusNames=STK_22980 {ECO:0000312|EMBL:BAB67409.1};
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, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP LYS-125 AND LYS-173.
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) IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S); MAGNESIUM ION AND THIAMINE PYROPHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-49, COFACTOR,
RP SUBUNIT, AND SUBSTRATE 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: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 -!- 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 -!- 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}.
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DR EMBL; BA000023; BAB67409.1; -; Genomic_DNA.
DR RefSeq; WP_010980384.1; NC_003106.2.
DR PDB; 5B48; X-ray; 2.50 A; B/D=1-305.
DR PDBsum; 5B48; -.
DR AlphaFoldDB; Q96Y68; -.
DR SMR; Q96Y68; -.
DR STRING; 273063.STK_22980; -.
DR EnsemblBacteria; BAB67409; BAB67409; STK_22980.
DR GeneID; 1460382; -.
DR KEGG; sto:STK_22980; -.
DR PATRIC; fig|273063.9.peg.2605; -.
DR eggNOG; arCOG01599; Archaea.
DR OMA; CSGKTSH; -.
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..305
FT /note="2-oxoacid:ferredoxin oxidoreductase 1, subunit beta"
FT /id="PRO_0000445532"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 44..47
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 91..92
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 122..123
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27619895,
FT ECO:0007744|PDB:5B48"
FT SITE 125
FT /note="Plays an important role in the binding of CoA"
FT /evidence="ECO:0000269|PubMed:19027887"
FT MUTAGEN 49
FT /note="K->I: Loss of oxidoreductase activity toward 2-
FT oxoglutarate but retains its activity toward pyruvate."
FT /evidence="ECO:0000269|PubMed:27619895"
FT MUTAGEN 125
FT /note="K->A: Shows a strong decrease of affinity for CoA
FT and a poor inactivation by 4-fluoro-7-nitrobenzofurazan
FT (NBD-F)."
FT /evidence="ECO:0000269|PubMed:19027887"
FT MUTAGEN 173
FT /note="K->A: Same oxidoreductase activity as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:19027887"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:5B48"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:5B48"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5B48"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:5B48"
SQ SEQUENCE 305 AA; 33636 MW; 57708EE7A2EB67F4 CRC64;
MAAFKPQWND WCPGCGNFGI LNAEQQAIVE LGVDTKNVVV VSGIGCSGKI PHFFRTPISG
VHTLHGRAIA FATGIKLSNP DLVVIVNGGD GDLLGIGAGH FVAAGRRNVD MVVILHDNGV
YGLTKGQASP TLKRGEKPKS LPRPNINDAV NPIALAISSG YTFVARGYAY DVKHLKELIK
SAIKHKGLAL IDVLQPCPTY NDINTKEWYD KRIYKLDTLP DWDPVVKKPE EVNEKIKRAI
DKSLEWGDRI PIGIFYQNEL VPSYEERIKA NSPAYLDYTP AKQLIEKEGK LTTIIDPLLK
EREVD
