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
//