GenomeNet

Database: UniProt
Entry: I3TFW6_THEC1
LinkDB: I3TFW6_THEC1
Original site: I3TFW6_THEC1 
ID   I3TFW6_THEC1            Unreviewed;       275 AA.
AC   I3TFW6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE            EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN   OrderedLocusNames=TCELL_1231 {ECO:0000313|EMBL:AFK51654.1};
OS   Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Thermogladius.
OX   NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK51654.1, ECO:0000313|Proteomes:UP000005270};
RN   [1] {ECO:0000313|EMBL:AFK51654.1, ECO:0000313|Proteomes:UP000005270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22663 / VKM B-2946 / 1633
RC   {ECO:0000313|Proteomes:UP000005270};
RX   PubMed=22843584; DOI=10.1128/JB.00894-12;
RA   Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA   Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the hyperthermophilic cellulolytic
RT   Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL   J. Bacteriol. 194:4446-4447(2012).
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:0000256|ARBA:ARBA00000005};
CC   -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC       {ECO:0000256|ARBA:ARBA00011631}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003531; AFK51654.1; -; Genomic_DNA.
DR   RefSeq; WP_014737904.1; NC_017954.1.
DR   AlphaFoldDB; I3TFW6; -.
DR   STRING; 1184251.TCELL_1231; -.
DR   GeneID; 13013551; -.
DR   KEGG; thg:TCELL_1231; -.
DR   eggNOG; arCOG01599; Archaea.
DR   HOGENOM; CLU_048564_2_0_2; -.
DR   InParanoid; I3TFW6; -.
DR   OMA; PTIFCPG; -.
DR   OrthoDB; 30755at2157; -.
DR   Proteomes; UP000005270; Chromosome.
DR   GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005270}.
FT   DOMAIN          70..208
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   275 AA;  30327 MW;  8625836088EF9CE3 CRC64;
     MALAKLTLHP LDKYLRTDRL PHIWCPGCGI GIALGAMLRA IDRRINEGRL DRNKVVFVTG
     IGCSARVSFY VDFDSAHTLH GRALPFATGV KLANPSLEVI VVGGDGDVAG IGGNHLLHAA
     KRNIDLFVVM ITNFVYAMTG GQLAPTTPLK VYTTTTPHGN PEPPLNVIKL VASLNANYVA
     RASITTPHYI EMFTYKALGM KGFRFLEVIS TCPEVYGRHI GLRNPVTMFE ELKKRVKYKP
     NPVIDESDID WEKGIVIGEY VVRNNPSYLD LVKRG
//
DBGET integrated database retrieval system