OFOB2_AERPE
ID OFOB2_AERPE Reviewed; 309 AA.
AC Q9YBX8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 2, subunit beta {ECO:0000303|PubMed:15848165};
DE Short=OFOR2 {ECO:0000303|PubMed:15848165};
DE EC=1.2.7.11 {ECO:0000269|PubMed:15848165};
GN OrderedLocusNames=APE_1472 {ECO:0000312|EMBL:BAA80470.1};
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q96XT4};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q96XT4};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q96XT4};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:Q96XT4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96XT4};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:Q96XT4};
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}.
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DR EMBL; BA000002; BAA80470.1; -; Genomic_DNA.
DR PIR; H72626; H72626.
DR AlphaFoldDB; Q9YBX8; -.
DR SMR; Q9YBX8; -.
DR STRING; 272557.APE_1472; -.
DR EnsemblBacteria; BAA80470; BAA80470; APE_1472.
DR KEGG; ape:APE_1472; -.
DR PATRIC; fig|272557.25.peg.997; -.
DR eggNOG; arCOG01599; Archaea.
DR OMA; PEWCPGC; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019164; F:pyruvate synthase activity; IDA:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; ISS: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 Iron; Iron-sulfur; Magnesium; Metal-binding; Oxidoreductase;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..309
FT /note="2-oxoacid:ferredoxin oxidoreductase 2, subunit beta"
FT /id="PRO_0000445538"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 49..52
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 68
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 94..95
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 125..126
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 200
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT SITE 128
FT /note="Plays an important role in the binding of CoA"
FT /evidence="ECO:0000250|UniProtKB:Q96Y68"
SQ SEQUENCE 309 AA; 34411 MW; 94DD12887449781D CRC64;
MARSWLDYKT QAWVQWCPGC GDFGILNSIY RAVSELGIDP ENLAVVGGIG CSGRTTYYVK
GSNFHALHGR AIPVATGVKL ANPHLNVIVA GGDGDLMGIG GGHFVALGRR NLNITVLLFD
NAVYGLTKGQ AAPTLPAWVK TKALSMPNIH DNINPVLLAF AAGYTFIARG YAYHTQQLKE
LIKTAVRHRG AALVDILQPC PTYNNIMTNK WYEERIYYVD QEEGYDPIIR TPEEFQKKAP
AIAAKLMEFG DRIPLGILYW NQTRESFEER LEKIMPGYMS APPATRRIEL EGKPFLHPFD
IFKDRLVTP
