ID A8MDG0_CALMQ Unreviewed; 553 AA.
AC A8MDG0;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Cmaq_0984 {ECO:0000313|EMBL:ABW01816.1};
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW01816.1, ECO:0000313|Proteomes:UP000001137};
RN [1] {ECO:0000313|EMBL:ABW01816.1, ECO:0000313|Proteomes:UP000001137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC {ECO:0000313|Proteomes:UP000001137};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000852; ABW01816.1; -; Genomic_DNA.
DR AlphaFoldDB; A8MDG0; -.
DR STRING; 397948.Cmaq_0984; -.
DR KEGG; cma:Cmaq_0984; -.
DR eggNOG; arCOG01998; Archaea.
DR HOGENOM; CLU_013748_3_1_2; -.
DR Proteomes; UP000001137; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001137};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..96
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 60273 MW; 23B53A086317E310 CRC64;
MRDLVSEWLI NNVGNYVFTV AAENILGLLR SLINRGGFII NSKFEPSAGF MALVSSRLLL
KPSTLIVTAG PGIFGALSPI AEAFIEGDPL IVIATSIIGG KGTRMHQIRD DTQLNTLSNV
VKASLRVSNP SNVTEVLTKA YRIATSGKPG PVYIDIPSDL MDLDTTGERK DVNPVTGETV
AINNDAVKEA ANLLSNAELP VLLLGRGVIL SGAKDLAIKL AELLNAPITT TIMAKGLISP
NHPLYAGVAA GKAGNMTAYE IIKKADVVLA IGNRFSEIGT GRYSLEIRGK LIHVNIDEYD
LGRAYEPYLR IRADAKEFLL MLINVLKGMS IRRRGGVINE LRELWSIENR ELNSYYEKAT
GLIKPWEVIR AVRDVFNKGG SIFIGDVGAH RIESFLMPIN ENEHYVTSTS YVSMGLAVPG
AVAASIIYRD RDVVALVGDG GFLMTGLEVA TAVQYGVKPK IIVFNDSAYR VLRIYEKVRF
SNATESLIKL PSIDFNLLAE SLGAEGLRIT RREELRPLLN EALNSDKATI VDVHIDPNTI
PIPYQRLYGL NTI
//
