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Database: UniProt
Entry: U9UI67_RHIID
LinkDB: U9UI67_RHIID
Original site: U9UI67_RHIID 
ID   U9UI67_RHIID            Unreviewed;       566 AA.
AC   U9UI67;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLOINDRAFT_75212 {ECO:0000313|EMBL:ESA20050.1};
OS   Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS   (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA20050.1};
RN   [1] {ECO:0000313|EMBL:ESA20050.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA20050.1};
RG   DOE Joint Genome Institute;
RA   Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA   Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA   Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA   Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA   Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA   San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA   Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA   Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT   "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT   evolution of the oldest plant symbiosis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; KI277703; ESA20050.1; -; Genomic_DNA.
DR   AlphaFoldDB; U9UI67; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_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; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..108
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..314
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          396..519
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         25
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         112
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         153
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         475
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ   SEQUENCE   566 AA;  63459 MW;  7E45EA8D1F7D3596 CRC64;
     MRIGEYLIKR LKQLGVKHLF GVPGDFNLKF LDLVEDDEGI EWIGGCNELN IGYAADGYAR
     INKIGAVVTT FGVGELSVIN AIAGSYAEMV PVVHIVGTPS TQSQADGAIL HHTLGNGDFR
     IYMKMYEGIT VAQTSLNQDN AKSEIDRVLR ECYIKARPVY ISLPTDVYNK DIDVAEDLSD
     DPLDLSYPEN PREVEEAAIS QIIEEIHKSK STIILADVGT SRYSITKEFV NFAEKTGFRV
     FTSPMGKGVI SENHPLFGGI YIGNVSEPHV QHGVEEADLI ISIGSLKSDF NTGGFSYLVS
     AAKTIELRHD RVTVFYAVYE NVSMRQILPK LTSRLERQPD LTQIESPYQS QPVMEELSSQ
     QITHSWFWRE IASKFLKPND IIIAETGTSM FGLMDVRFPE GATFISQILY GSIGYSVGAT
     LGATLAVKNG KTKRRVILFV GDGSFQVTVQ EVSTMIRNNL DPIIFIINND GYTIERLIHG
     LKRKYNDIQP WQYCKTLEYF STTRKGRTIQ VSTKKEFESC ISQLSDSPFN EIQIIEIIMD
     KFDAPRSLLK TTENTYKEIP PEMQKK
//
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