GenomeNet

Database: UniProt
Entry: D8MVC6_ERWBE
LinkDB: D8MVC6_ERWBE
Original site: D8MVC6_ERWBE 
ID   D8MVC6_ERWBE            Unreviewed;       550 AA.
AC   D8MVC6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Indolepyruvate decarboxylase {ECO:0000313|EMBL:CAX60783.1};
DE            EC=4.1.1.74 {ECO:0000313|EMBL:CAX60783.1};
GN   Name=ipdC {ECO:0000313|EMBL:CAX60783.1};
GN   OrderedLocusNames=EbC_32520 {ECO:0000313|EMBL:CAX60783.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX60783.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX60783.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|ARBA:ARBA00001920};
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}.
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; FP236843; CAX60783.1; -; Genomic_DNA.
DR   RefSeq; WP_013203268.1; NC_014306.1.
DR   AlphaFoldDB; D8MVC6; -.
DR   STRING; 634500.EbC_32520; -.
DR   KEGG; ebi:EbC_32520; -.
DR   eggNOG; COG3961; Bacteria.
DR   HOGENOM; CLU_013748_0_2_6; -.
DR   OMA; EQRYNDI; -.
DR   Proteomes; UP000008793; Chromosome.
DR   GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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, ECO:0000313|EMBL:CAX60783.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:CAX60783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..108
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          382..526
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   550 AA;  58693 MW;  E2D4CB875505C20B CRC64;
     MQSLTVGEYL LSRLWEAGIG HLFGVPGDYN LQFLDDVITS SEIGWVGCAN ELNAAYAADG
     YARCHGAAAL LTTFGVGELS ALNGVAGSYA EYLPVIHIVG APATAAAREG LLLHHTLGDG
     DYRHFMRMSQ EVTVAQAILT PENAVEEIDR LLIAALHERR PVYLYLATDV AVAKIIPAAT
     PLATERPCDA ATVAAFADAA DQLLAGAKNV AMLADFLADR AQQQGKLKQL LTDAPMPFAT
     LLMGKGVLPE QHTGFAGTYA GAASAGHTQQ IIEQADVLIT VGVLYTDTIT AGFTQNIDSA
     KTLAIGLSSS RIGDKTFTQL PMSAALTALH PLVKRYAAQW PEPEVSPPPL NDVPSDALTQ
     DSFWQAIQHF LKPGDIVLAD QGTSAFGAAA LRLPEGVTFI SQPLWGSIGY TLPAAYGAQV
     ACPDRRVVLL SGDGSAQLTI QELGSMLRDG MKPVIFILNN AGYTVERAIH GEHQRYNDIA
     AWNWTQLPQA LSLNCAAQSW RVEQTVQLVE VMKVIAQSDR LSLVEVVLPP LDVPPLLQAV
     CEALNKRNSA
//
DBGET integrated database retrieval system