ID A3MTB7_PYRCJ Unreviewed; 549 AA.
AC A3MTB7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pcal_0451 {ECO:0000313|EMBL:ABO07884.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO07884.1, ECO:0000313|Proteomes:UP000001431};
RN [1] {ECO:0000313|EMBL:ABO07884.1, ECO:0000313|Proteomes:UP000001431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1
RC {ECO:0000313|Proteomes:UP000001431};
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-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; CP000561; ABO07884.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MTB7; -.
DR STRING; 410359.Pcal_0451; -.
DR KEGG; pcl:Pcal_0451; -.
DR eggNOG; arCOG01998; Archaea.
DR HOGENOM; CLU_013748_3_1_2; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000001431; 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 GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ABO07884.1}.
FT DOMAIN 1..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 549 AA; 60108 MW; CD7D7D8D56976001 CRC64;
MNVAEAVVKC LEQLGVKRVY GLIGTSILDF VDALRDSKIR YISTRHEQVA VSMADAEGRI
TGRPGVAAVH AGPGFLNSLI SVAAAYKDVS PLLLISGAVK RRLAGLDSWL EVPQRDIIRP
LVKGVYRVDK PLEIGKVISE AYSLAASPPQ GPVFVEVPED VWNMSSQAEK CEVKIAPPPT
VPKDFVDKVA ELLSKSKRPL ILAGGGVNNE EGRRLLLDVS ERWKIPVAVT GNGRGAYPED
HPLFLGKVGF GGGNIVADRA LVEADLVLAV GAGLSDTTTY GYNFVPRGDI VAVNLDPLAE
KKPVPYTLYH YADAVDFLKK LAALDLKYEP SVEWFREIEE WKAAWNALLS EALSRSYKGF
VNPSKFFHRL NKSLPRDFVM VGGQGMHLVY TFAFITVKAV RGYLAAFNLG AMGFAFPAAL
GAKVVAPERD VYAVLGDGEF MMTVQDLETA VREKIGVKII VVNDNAYRVL YARQKAQKMG
RIYGTLHTNP DFVKLAEAFG VEAMSISQDE EIEKAVNFIT RPTDKPLLLE LKIHPDDLPP
MNIDGALRF
//
