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Database: UniProt
Entry: A0A060M0W7_9BACI
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Original site: A0A060M0W7_9BACI 
ID   A0A060M0W7_9BACI        Unreviewed;       551 AA.
AC   A0A060M0W7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Pyruvate decarboxylase {ECO:0000313|EMBL:AIC95670.1};
GN   ORFNames=BleG1_3106 {ECO:0000313|EMBL:AIC95670.1};
OS   Shouchella lehensis G1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95670.1, ECO:0000313|Proteomes:UP000027142};
RN   [1] {ECO:0000313|EMBL:AIC95670.1, ECO:0000313|Proteomes:UP000027142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:AIC95670.1,
RC   ECO:0000313|Proteomes:UP000027142};
RX   PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA   Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA   Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA   Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT   "A comparative genomic analysis of the alkalitolerant soil bacterium
RT   Bacillus lehensis G1.";
RL   Gene 545:253-261(2014).
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; CP003923; AIC95670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060M0W7; -.
DR   STRING; 1246626.BleG1_3106; -.
DR   KEGG; ble:BleG1_3106; -.
DR   PATRIC; fig|1246626.3.peg.3099; -.
DR   eggNOG; COG3961; Bacteria.
DR   HOGENOM; CLU_013748_0_2_9; -.
DR   Proteomes; UP000027142; 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   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}; Pyruvate {ECO:0000313|EMBL:AIC95670.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027142};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          8..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          392..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         436
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   551 AA;  61598 MW;  C31C9C9D2A0FFC61 CRC64;
     MDRANQQTVG DYLYESLYKE GIRDVFGVPG DYNFALLDTL ERTDSLRFIH NRNELNAGYA
     ADGYARLHGI SALITTFGVG ELSAANAIAG ANCENIPIIH IVGAPDYDKQ EKGLHVHHTL
     MNGDFHVFKR MFTEISAYST VVTPSNAKTE VEKAIQMAKD YQKPVYIMVA DDHVNELVTE
     KDGEGIVPFE TDKETFAQAM RHIEKKVSDS KKPILLVDTK VKSFELEQLI QKVTESLRIP
     VASMVYGKGS VDESSDQYIG MYAGNFGSHE VRDRVEHADC VIGVGLVWAD TNTANYTASL
     RKEQLIDIQP HYVRVEHATY ENVKASDVLK EVGTLETSID TVASPITFPY ATALETEDKA
     LRASNYYPIL QDFIQEEDIV IVETGTFFYG MSQARMKKGV SYLKQGGWQS IGFATAATFG
     ASIAEPNRRT LLFTGDGSMQ LTVQEISSML YYDCKPIIFV LNNAGYTIER YLNTETKEQV
     YNDIPTWNYS SLLEGFGGGA KHVKAKTTAE LQHVLRQVEK DDCLCVVEII VDDPMDAPDY
     VKQIRAFKKE E
//
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