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Database: UniProt
Entry: A9MIH1_SALAR
LinkDB: A9MIH1_SALAR
Original site: A9MIH1_SALAR 
ID   A9MIH1_SALAR            Unreviewed;       550 AA.
AC   A9MIH1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Indolepyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SARI_00479 {ECO:0000313|EMBL:ABX20408.1};
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX20408.1, ECO:0000313|Proteomes:UP000002084};
RN   [1] {ECO:0000313|EMBL:ABX20408.1, ECO:0000313|Proteomes:UP000002084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC   {ECO:0000313|Proteomes:UP000002084};
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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=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}.
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DR   EMBL; CP000880; ABX20408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MIH1; -.
DR   STRING; 41514.SARI_00479; -.
DR   KEGG; ses:SARI_00479; -.
DR   HOGENOM; CLU_013748_0_2_6; -.
DR   OMA; EQRYNDI; -.
DR   Proteomes; UP000002084; Chromosome.
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   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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000002084};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..114
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          202..323
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          392..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;  59957 MW;  60263295EB7D8D63 CRC64;
     MQTPYTVADY LLDRLAGCGI GHLFGVPGDY NLQFLDHVID HPTLRWVGCA NELNAAYAAD
     GYARMSGAGA LLTTFGVGEL SAINGIAGSY AEYVPVLHIV GAPCSAAQQR GELMHHTLGD
     GDFHHFYRMS QAISAGSAIL NEQNACFEID RVLGEMVAAR RPGYIMLPAD VAKKTAIPPI
     EALTLPAHET QNGVETAFRY RARQCLMNSR RIALLADFLA RRFGLRPLLQ RWMAETSIAH
     ATLLMGKGLF DEQHPNFVGT YSAGASSKAV RQAIEDADMV ICVGTRFVDT LTAGFTQQLP
     AERTLEIQPY ASRIGETWFN LPMAQAVSTL RELCLECAFA PPPTRPVCQP VQIEKGELTQ
     ENFWQTLQQY LKPGDIILVD QGTAAFGAAA LSLPDGAEVV VQPLWGSIGY SLPAAFGAQT
     ACPDRRVILI IGDGAAQLTI QEMGSMLRDG QAPIILLLNN DGYTVERAIH GAAQRYNDIA
     SWNWTQIPQA LNAAQQAECW RVTQAIQLAE VLERLARPQR LSFIEVMLPK ADLPELLRTV
     TRALEARNGG
//
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