ID I9WCJ2_9SPHN Unreviewed; 559 AA.
AC I9WCJ2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Thiamine pyrophosphate binding domain-containing protein {ECO:0000313|EMBL:EIZ77908.1};
GN ORFNames=WSK_3579 {ECO:0000313|EMBL:EIZ77908.1};
OS Novosphingobium sp. Rr 2-17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ77908.1, ECO:0000313|Proteomes:UP000004732};
RN [1] {ECO:0000313|EMBL:EIZ77908.1, ECO:0000313|Proteomes:UP000004732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX PubMed=22933764; DOI=10.1128/JB.01159-12;
RA Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL J. Bacteriol. 194:5137-5138(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}.
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:EIZ77908.1}.
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DR EMBL; AKFJ01000110; EIZ77908.1; -; Genomic_DNA.
DR RefSeq; WP_008996503.1; NZ_AKFJ01000110.1.
DR AlphaFoldDB; I9WCJ2; -.
DR PATRIC; fig|555793.3.peg.3521; -.
DR eggNOG; COG3961; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000004732; 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; 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; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000004732};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..109
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..297
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 559 AA; 60727 MW; 8EAD9F7A87429AB5 CRC64;
MDHETTVGQY LVDRLSEIGL RHLFSIAGDY SIEWLNRYVT PSKIALIEEV NELNAGYAAD
AYARMRGIGA LCTTYSAGSL CAVNPVAGAY VEKVPLVLIA GTPSIKRTLT FEQTGFCAHH
FIAGRQTDLQ VFQYITVATI RLDDPDAAPG LIDYALRACI SQKRPVYIEL LQDIVDLPCP
AAQDCLTRSR MLCSEPDLGD AIKAIAPKLA AASKPLLWLG VEINRFGLSG LALQLVEHFQ
IPFVTELMSK SVLSEDHPLF AGVFDGQSSS GQVQSLMAQA DVVLALGIWL TDINDLGGGV
DTAKTVFASF DTVKHGPDFW AQVTLDRFIK ALLTVERPSA SGSFTRIETA PDIEANPCAA
ITYDGFYDIL PDYIDAHTIV SCDASLNYFG AIRLKVPGPG NFFAQTSYSA IGYAGPAATG
LCLAREDGGK VLVLSGDGGF QMTAQCLSTQ TRFGLDPIIF IMDNGSYAVE QWLANAAYFA
TDKPFYESCR LHRWDYAQLA GVFGCRGWRV QTRDELRKAV ADAMSNKDSP SIIQVMLPDK
DLPANARWKI AIDAQTAPP
//