ID H6NDK2_9BACL Unreviewed; 575 AA.
AC H6NDK2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Thiamine pyrophosphate protein TPP binding domain-containing protein {ECO:0000313|EMBL:AFC31342.1};
GN ORFNames=PM3016_4596 {ECO:0000313|EMBL:AFC31342.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC31342.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC31342.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC31342.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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; CP003235; AFC31342.1; -; Genomic_DNA.
DR RefSeq; WP_014371071.1; NC_016935.1.
DR AlphaFoldDB; H6NDK2; -.
DR STRING; 1116391.PM3016_4596; -.
DR KEGG; pmq:PM3016_4596; -.
DR HOGENOM; CLU_013748_0_2_9; -.
DR Proteomes; UP000007523; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007523};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 22..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 575 AA; 62306 MW; 49F7EDE3AFEF9076 CRC64;
MSAKTDKDRS SAGRAEEAAV SLGRFLFDSL KREGVTEIFG VPGDYNFTLL DELERCEGMR
FIGGRNELNA GYAADSYARL RGLGALITTF GVGEMSAANA VAGAYSESVP LVHIVGTPKS
AAQRERRLMH HSLLDGDYEV FRRAYGEITA YTAVLTPENA AAEIPKAIRT AKEKKKPVYL
AVAIDLVDRP VVVQAHGEPE PKLQRRTDPA VLEAASAHAK RLLGAAGRAV ILSDLPVQRF
GLGEPVQRLA EALNVPAAST MLGKGSFDEG HPNYIGVYGG EFGSEDVRSI VEEAGCLIAV
GLVRSDGNLA NFTAKLDTAQ LIEIQPDSVR IGEALYPGIR AEEMLRALEE SGFRGGELPR
VRHPYDEPAG GPGDAVTAKT YLPRFQRMLK EGDVVVVETG TLAYGMSEVR LPKGAAYIHQ
GAWQSIGYAL PAAFGAAVAD PQRRIVLFTG DGALQLTVQE ISSMLACGGR LILFVLNNRG
YTIEKYLNVR TERQPYNDIP EWSYTRLAEA FGGEAYTARV RTNGELDAAM AEAEAQCGRR
LCLIELVPED PMDAPPYLKR KRSYLEAQEA QRAKG
//
