ID A4XUU7_PSEMY Unreviewed; 598 AA.
AC A4XUU7;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABP85113.1};
GN OrderedLocusNames=Pmen_2355 {ECO:0000313|EMBL:ABP85113.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP85113.1};
RN [1] {ECO:0000313|EMBL:ABP85113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP85113.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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; CP000680; ABP85113.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XUU7; -.
DR STRING; 399739.Pmen_2355; -.
DR KEGG; pmy:Pmen_2355; -.
DR PATRIC; fig|399739.8.peg.2378; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR OrthoDB; 9785953at2; -.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-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; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 598 AA; 65428 MW; 7D4EAB0117581AED CRC64;
MAMTVGDFIV ERLYQWGVRR IYGYPGDGIN GVFGALNRAD GKIRFIQARH EEMAAFMAAA
DAKFSGQLGV CIATSGPGAT HLLTGLYDAR MDHMPVLAIT GQQARTALGG HYQQELDLVS
VFKDVAGAFV QQASAPAQVR HLVDRAIRTA IGERRVTAII LPNDLQEAEY TEPPHKHGTV
HSGIGYSRPR VVPYEADLQR AAEVLNSGKK VAMLVGAGAL NAGDEVFEVA QKLGAGVAKA
LLGKAVLPDD LPWVTGSIGL LGTVPSYKMM EECDTLLMIG SGFPYSEFLP QEGKARGVQI
DIQPDMLSLR YPMEVNLVGD AAETLRALLP LLEDKQERSW RATIEDWRSD WDRTLEKRAM
VSAKPINPQR VVYELSPRLP ERAIVTCDSG SCANWYARDL KIRRGMSCSL SGGLASMGAA
VPYAIAAKFA HPDRPVVGLV GDGAMQMSNL AELITVAKYW REWENPQWVL AVFNNQDLNQ
VTWEQRVMEG DPKFEASQDI PDVPYHAFAN SIGLTGVLIE REEDVGPAWE QALAAERPVL
LEFRTDPDVP PLPPHISLEQ AKQFASTLLQ GDPDQRGILA QTAKQLFGAL LPGKRKDN
//
