ID A5W220_PSEP1 Unreviewed; 535 AA.
AC A5W220;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABQ78180.1};
GN OrderedLocusNames=Pput_2040 {ECO:0000313|EMBL:ABQ78180.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ78180.1};
RN [1] {ECO:0000313|EMBL:ABQ78180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ABQ78180.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000712; ABQ78180.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W220; -.
DR KEGG; ppf:Pput_2040; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 535 AA; 56946 MW; CF61D6613CD72D79 CRC64;
MNDLTLTAGQ ALVRLLANYG VETVFGIPGV HTLELYRGLP GSGIRHVLTR HEQGAGFMAD
GYARVSGKPG VCFVITGPGV TNVATPIGQA YADSVPMLVI SSVNHTASLG KGWGCLHETQ
DQRAMTAPIT AFSAVALRGD DLPELIARAW AVFDSERPRP VHISVPLDVL AAPVSRDWSD
EVVRRPERGQ PCRESLDQAA LKLAAAERPM IIAGGGALHA AEQLAQLSAR LAAPVFTSVA
GKGLLPPQAP LNAGSSLCVE PGWQLISQAD VVLAVGTEMA DTDFWRERLP ITGELLRVDI
DPRKFNDFYP CAIALQGDAR QTLAGLLEHL PALDRDPAQA SEAVSDLRQA IRHGHAPLQA
IHQAILDRIA AVLPDDAFIS SDMTQLAYTG NYAFASRAPR SWLHPTGYGT LGYGLPAGIG
GMLATDHRPG LVLVGDGGFL YTAQELATAV EELDRPLVVL LWNNDALGQI RDDMLGLNIE
PVGVLPRNPD FIGLARAFGC AVRQPRDLDA LQADLASGFA TPGVTFIELK HTCVC
//
