OFOB1_AERPE
ID OFOB1_AERPE Reviewed; 318 AA.
AC Q9YA11;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase 1, subunit beta {ECO:0000303|PubMed:15848165};
DE Short=OFOR1 {ECO:0000303|PubMed:15848165};
DE EC=1.2.7.11 {ECO:0000269|PubMed:15848165};
GN OrderedLocusNames=APE_2128 {ECO:0000312|EMBL:BAA81139.1};
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 and glyoxylate
CC to form their CoA derivatives. {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=240 uM for pyruvate (at 80 degrees Celsius)
CC {ECO:0000269|PubMed:15848165};
CC Vmax=10.1 umol/min/mg enzyme with pyruvate as substrate (at 80
CC degrees Celsius) {ECO:0000269|PubMed:15848165};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:15848165};
CC Temperature dependence:
CC Optimum temperature is 105 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; BAA81139.1; -; Genomic_DNA.
DR PIR; C72519; C72519.
DR AlphaFoldDB; Q9YA11; -.
DR SMR; Q9YA11; -.
DR STRING; 272557.APE_2128; -.
DR EnsemblBacteria; BAA81139; BAA81139; APE_2128.
DR KEGG; ape:APE_2128; -.
DR PATRIC; fig|272557.25.peg.1417; -.
DR eggNOG; arCOG01599; Archaea.
DR OMA; CSGKTSH; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate 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..318
FT /note="2-oxoacid:ferredoxin oxidoreductase 1, subunit beta"
FT /id="PRO_0000445536"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 50..53
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 69
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 95..96
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 126..127
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT SITE 129
FT /note="Plays an important role in the binding of CoA"
FT /evidence="ECO:0000250|UniProtKB:Q96Y68"
SQ SEQUENCE 318 AA; 34937 MW; 8406198FA334B88C CRC64;
MASRGVASYR TEVWSDWCPG CGDFGILAAM QKAFAELNLD PAQTVVVSGI GCSSKTPHFI
NVNGVHTIHG RGIAFATGIK LANPQLKVIV NGGDGDLLGI GVAHFVALGR RNLDVTVLIH
NNKVYGLTKG QASPTLRRGE KVKSLPVPNL QDAVNPIALA IASGYTFVAR AYSLWVDHLK
EILKAAINHK GSAVIDVLQP CVTYNDIYTA EFYKDRLYKL EDDPSWDPIV RDPSEDEEKK
AAAIKKAEEW GTRIPVGVFY VNPLKDTYEE RLAQRNPSYS IDNPPALQPI SREDGSPIVG
PDEFRKIFKR FIVNVKKL
