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Database: UniProt
Entry: A8GKW2_SERP5
LinkDB: A8GKW2_SERP5
Original site: A8GKW2_SERP5 
ID   A8GKW2_SERP5            Unreviewed;       646 AA.
AC   A8GKW2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   28-MAR-2018, entry version 70.
DE   SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:ABV43752.1};
GN   OrderedLocusNames=Spro_4659 {ECO:0000313|EMBL:ABV43752.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV43752.1, ECO:0000313|Proteomes:UP000007074};
RN   [1] {ECO:0000313|EMBL:ABV43752.1, ECO:0000313|Proteomes:UP000007074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV43752.1,
RC   ECO:0000313|Proteomes:UP000007074};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000826; ABV43752.1; -; Genomic_DNA.
DR   RefSeq; WP_012147334.1; NC_009832.1.
DR   ProteinModelPortal; A8GKW2; -.
DR   STRING; 399741.Spro_4659; -.
DR   EnsemblBacteria; ABV43752; ABV43752; Spro_4659.
DR   KEGG; spe:Spro_4659; -.
DR   eggNOG; ENOG4107QK6; Bacteria.
DR   eggNOG; COG3962; LUCA.
DR   HOGENOM; HOG000239708; -.
DR   KO; K03336; -.
DR   OMA; LPKTMTH; -.
DR   OrthoDB; POG091H02KO; -.
DR   Proteomes; UP000007074; Chromosome.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; 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:0019310; P:inositol catabolic process; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_iolD.
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-bd_C.
DR   PANTHER; PTHR18968:SF9; PTHR18968:SF9; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007074};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        8    196       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      220    353       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      442    601       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   646 AA;  70660 MW;  2431A00040C80DA2 CRC64;
     MGKIRLTMAQ ALVRFLDNQY LVVDGVETKF VKGIFAIFGH GNVLGLGQAL EQDSGDLIVH
     QGRNEQGMAH AATGFAKQKL RQQIYACTSS VGPGAANMIT AAATATANRI PLLLLPGDVY
     ASRQPDPVLQ QIEQSYDLSI STNDAFRAVS KYWDRIVRPE QLMSACINAM RVLTDPAETG
     AVTLSLPQDV QGEAYDYPDY FFQKRVHRLD RRPATEGMLA DALALLTTKR QPLLVCGGGV
     KYSQAGQALR EFAERFRIPF VETQAGKGTV PSNHPFNLGG IGETGCLAAN TLARQADLVI
     GVGTRYTDFT TSSKWLFQHP DVDFLNVNVS AFDAGKLDGL QVLADAREAL SALGALLAQA
     DYRAGWGNAI AEARSAQQQE TARVYAVEYT GEGFVPEIDD HLDRDSVFAE FIEKTDSLLT
     QSRVLGVLNQ HLPQDSVIVA AAGSLPGDLQ RVWQNHGEHG YHVEYGYSCM GYEVNAALGV
     KLAEPQREVY AMVGDGAFMM LHSELVTSIQ EGCKINVVLF DNMTNGCINN LQMEHGMDSY
     TTEFRFRNPQ GGKLDGKLVP VNFAMLAAAY GCKTYSVTTE QQLIEALADA RLQSVSTLLD
     IKVLPKTMVH KYLSWWRVGG AQVADSEKIV AVARKLQENI DKARDY
//
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