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Database: UniProt
Entry: A0A0M5JJZ2_9BACI
LinkDB: A0A0M5JJZ2_9BACI
Original site: A0A0M5JJZ2_9BACI 
ID   A0A0M5JJZ2_9BACI        Unreviewed;       566 AA.
AC   A0A0M5JJZ2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:ALC89289.1};
GN   ORFNames=AM500_05430 {ECO:0000313|EMBL:ALC89289.1};
OS   Bacillus sp. FJAT-18017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC89289.1, ECO:0000313|Proteomes:UP000060713};
RN   [1] {ECO:0000313|EMBL:ALC89289.1, ECO:0000313|Proteomes:UP000060713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC89289.1,
RC   ECO:0000313|Proteomes:UP000060713};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-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=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; CP012602; ALC89289.1; -; Genomic_DNA.
DR   RefSeq; WP_053598320.1; NZ_CP012602.1.
DR   AlphaFoldDB; A0A0M5JJZ2; -.
DR   STRING; 1705566.AM500_05430; -.
DR   PATRIC; fig|1705566.3.peg.1166; -.
DR   Proteomes; UP000060713; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000060713};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          17..126
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          210..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          400..533
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   COILED          512..539
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         445
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   566 AA;  63159 MW;  6111B1C49F0BFF9A CRC64;
     MTSMDNSSQQ IPMGQKTVGE YLFDCLKQEG ITEIFGVPGD YNFTLLDALQ EYNGIRFYNG
     RNELNAGYAA DGYARIKGIS ALITTFGVGE LSATNAIAGA NSEHVPIIHI VGSPPEKAQK
     ERKLMHHTLM DGNFDVFRKV YEPLTAYTTI VTADNARMEI PAAIRIAKER RKPVYLVVAD
     DVVAKPITGR EVPASPLPAS NQDKLLAAVE HVRRLLEPAR QPVILVDVKA MRFGLQTAVR
     ELANTMNVPV ATMMYGKGTF DETHPNYIGV YAGTFGSSEV QSIVENSDCV IAVGLVWSDT
     NTANFTAKLN PHNTIEVQPT KVKIAESQYP DVRAADILQE MQKLDYRSQS KPEKISFPYE
     EITGSSDEPL RAENYFPRFQ RMLKENDIVI AETGTFYYGM SQVKLPANTT YIMQGGWQSI
     GYATPAAYGA SIAAPDRRVL LFTGDGSMQL TAQEISSMLY YGCKPIIFVL NNDGYTIERY
     LNVEISPDEQ NYNDIPNWSY TKLAEAFGGE LFTKTVRTNE ELDEAITQAE QEYAEKLCLI
     EMIAADPMDA PEYMHRIRNH KQEQKK
//
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