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Database: UniProt
Entry: A0A149Q9L7_9PROT
LinkDB: A0A149Q9L7_9PROT
Original site: A0A149Q9L7_9PROT 
ID   A0A149Q9L7_9PROT        Unreviewed;       563 AA.
AC   A0A149Q9L7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=AD928_08000 {ECO:0000313|EMBL:KXU93897.1};
OS   Acetobacter cerevisiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU93897.1, ECO:0000313|Proteomes:UP000075473};
RN   [1] {ECO:0000313|EMBL:KXU93897.1, ECO:0000313|Proteomes:UP000075473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU93897.1,
RC   ECO:0000313|Proteomes:UP000075473};
RA   Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT   "Improved classification and identification of acetic acid bacteria using
RT   matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT   heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT   respectively.";
RL   Submitted (JUN-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU93897.1}.
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DR   EMBL; LHZA01000144; KXU93897.1; -; Genomic_DNA.
DR   RefSeq; WP_062249646.1; NZ_LHZA01000144.1.
DR   AlphaFoldDB; A0A149Q9L7; -.
DR   PATRIC; fig|178900.5.peg.2512; -.
DR   Proteomes; UP000075473; Unassembled WGS sequence.
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:0044281; P:small molecule 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:SF6; PYRUVATE DECARBOXYLASE C186.09-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}; Pyruvate {ECO:0000313|EMBL:KXU93897.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075473};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..113
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          199..308
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          411..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
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"
SQ   SEQUENCE   563 AA;  60555 MW;  89E4FCC0391877B4 CRC64;
     MSYTVGTYLA ERLAQIGLKH HFAVAGDYNL VLLDQLLMNK ECEQVYCCNE LNCGFSAEGY
     ARANGAGAAV VTFSVGALSA LNAIGGAYAE NLPVILISAA PNSNDHGSGH ILHHTIGTTD
     YSYQLQIAEK LTCAAVSITS AEDAPEKIDH AIRTALREKK PAYIEIACNV SAQPCAAPGP
     ISAVVDAPAS NKATLDAAVK AVADFIEKHE KPAILVGSRL RAAGAEEAAV KLADALGCVV
     ATMAAAKSFF PEDHPSYVGT YWGSASTPGV NEIFNWTDSI IALAPIFNDY STEGWTAWPQ
     GPNVAVLDKN ITKLHGYAFD NIHLKELLEA LADYFKNKPK KDSTLVQYKR VHTERTVETT
     GKGDDVLTRA DIQQTLQSLV TPETTIVGET GDSWFNVMRT KLPRGARVEL EMQWGHIGWS
     VPAAFGYAVG APERRTILMV GDGSFQLTAQ EVAQMIRRKL PVIIFLINNA GYTIEVEIHD
     GPYNNIKNWD YAGIISAFNA EDGKGKGLRA NTAGELADAV KVALENKEGP TLIECVIPRD
     DCTSELISWG RHVATANGRP PAK
//
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