OFOB_SACSO
ID OFOB_SACSO Reviewed; 305 AA.
AC A0A0E3KBH3; A0A157T6A7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=2-oxoacid:ferredoxin oxidoreductase subunit beta {ECO:0000303|PubMed:16466637};
DE Short=OFOR {ECO:0000305};
DE EC=1.2.7.11 {ECO:0000269|PubMed:16466637};
GN ORFNames=SSOP1_2914 {ECO:0000312|EMBL:SAI86468.1},
GN SULA_0624 {ECO:0000312|EMBL:AKA78408.1},
GN SULB_0626 {ECO:0000312|EMBL:AKA73018.1},
GN SULC_0624 {ECO:0000312|EMBL:AKA75716.1};
OS Saccharolobus solfataricus (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98/2 SULC {ECO:0000312|EMBL:AKA75716.1,
RC ECO:0000312|Proteomes:UP000033057}, SULA {ECO:0000312|EMBL:AKA78408.1,
RC ECO:0000312|Proteomes:UP000033106}, and
RC SULB {ECO:0000312|EMBL:AKA73018.1, ECO:0000312|Proteomes:UP000033085};
RX PubMed=26021927; DOI=10.1128/genomea.00549-15;
RA McCarthy S., Gradnigo J., Johnson T., Payne S., Lipzen A., Martin J.,
RA Schackwitz W., Moriyama E., Blum P.;
RT "Complete Genome Sequence of Sulfolobus solfataricus Strain 98/2 and
RT Evolved Derivatives.";
RL Genome Announc. 3:E00549-E00549(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1
RC {ECO:0000312|EMBL:SAI86468.1};
RA Shah S.A., Garrett R.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
RX PubMed=16466637; DOI=10.5483/bmbrep.2006.39.1.046;
RA Park Y.J., Yoo C.B., Choi S.Y., Lee H.B.;
RT "Purifications and characterizations of a ferredoxin and its related 2-
RT oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon,
RT Sulfolobus solfataricus P1.";
RL J. Biochem. Mol. Biol. 39:46-54(2006).
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:16466637}.
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:16466637};
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=163 uM for 2-oxoglutarate {ECO:0000269|PubMed:16466637};
CC KM=275 uM for pyruvate {ECO:0000269|PubMed:16466637};
CC KM=516 uM for 2-oxobutyrate {ECO:0000269|PubMed:16466637};
CC Note=kcat is 452 min(-1) for 2-oxoglutarate as substrate. kcat is 144
CC min(-1) for pyruvate as substrate. kcat is 93 min(-1) for 2-
CC oxobutyrate as substrate.;
CC pH dependence:
CC Optimum pH is between 7-8. {ECO:0000269|PubMed:16466637};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:16466637};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:16466637}.
CC -!- MASS SPECTROMETRY: Mass=33600; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16466637};
CC -!- SEQUENCE CAUTION:
CC Sequence=SAI86468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP011055; AKA73018.1; -; Genomic_DNA.
DR EMBL; CP011056; AKA75716.1; -; Genomic_DNA.
DR EMBL; CP011057; AKA78408.1; -; Genomic_DNA.
DR EMBL; LT549890; SAI86468.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048186280.1; NZ_CP033241.1.
DR AlphaFoldDB; A0A0E3KBH3; -.
DR SMR; A0A0E3KBH3; -.
DR EnsemblBacteria; AKA73018; AKA73018; SULB_0626.
DR EnsemblBacteria; AKA75716; AKA75716; SULC_0624.
DR EnsemblBacteria; AKA78408; AKA78408; SULA_0624.
DR GeneID; 44128565; -.
DR KEGG; ssoa:SULA_0624; -.
DR KEGG; ssof:SULC_0624; -.
DR KEGG; ssol:SULB_0626; -.
DR PATRIC; fig|2287.9.peg.3055; -.
DR OrthoDB; 43666at2157; -.
DR Proteomes; UP000033057; Chromosome.
DR Proteomes; UP000033085; Chromosome.
DR Proteomes; UP000033106; Chromosome.
DR Proteomes; UP000076770; Chromosome i.
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 Thiamine pyrophosphate.
FT CHAIN 1..305
FT /note="2-oxoacid:ferredoxin oxidoreductase subunit beta"
FT /id="PRO_0000445528"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
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:0000250|UniProtKB:Q96XT4"
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:0000250|UniProtKB:Q96XT4"
FT BINDING 91..92
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 122..123
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q96XT4"
FT SITE 125
FT /note="Plays an important role in the binding of CoA"
FT /evidence="ECO:0000250|UniProtKB:Q96Y68"
FT CONFLICT 250
FT /note="T -> I (in Ref. 2; SAI86468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33616 MW; 89FABF906E2611CA CRC64;
MAGLKVEWND WCPGCGNFGI LSAEQQAIQE LGLDPKKVVL VSGIGCSGKI PHFIRLPASG
VHTLHGRALT FAIGIKLANP SLEVIVNGGD GDQLGIGVGH FVSAGRRNVD LTVIVHNNGV
YGLTKGQASP TLKLGVKTKS LPKPNINSDI NPIALAISSG YTFVARGYAY DVKHLKEIIK
KAIKHKGLAM IDVLQPCPTY NDIHTKEYYD KRVYKLDEDP SWDPIVKKPE EMDDKMSKAI
LKSMEWGDRT PIGIFYQNEL VSTYEQRIAE RSPSYLDNPP AHDVIEFEGK PTTDVEDILK
ERRVT
