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Database: UniProt
Entry: H5X7E8_9PSEU
LinkDB: H5X7E8_9PSEU
Original site: H5X7E8_9PSEU 
ID   H5X7E8_9PSEU            Unreviewed;       553 AA.
AC   H5X7E8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EHR50167.1};
GN   ORFNames=SacmaDRAFT_1908 {ECO:0000313|EMBL:EHR50167.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR50167.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR50167.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR50167.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CM001439; EHR50167.1; -; Genomic_DNA.
DR   RefSeq; WP_009153552.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5X7E8; -.
DR   STRING; 882083.SacmaDRAFT_1908; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_4_11; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000004926; Chromosome.
DR   GO; GO:0016874; F:ligase 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; 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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EHR50167.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004926};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          8..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          191..317
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..526
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          164..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  57143 MW;  421BBCE8A650CFB6 CRC64;
     MTVPSYAQEL AIAVAKTGCT HVFGLMGDGN MQLFVALRRQ GVHVVEVRHE SAAVAMAEGY
     GWSCDQVGIC SVTHGPGLSH VATSLLVAAR NRSPLVVIAA ETPAGYQGAQ TFDQQSFAEA
     CETRYRRMTQ GERPAQALAD AIESARDVSG PVILGVAADL LASTVDDSPA PGEPPAPTPG
     PPGLDDGAAA ERLTQLIAGS ARPVLIAGRG ATGGRSVGLL RTLAEHVGAG LATTLPAKGL
     FDGHHLDLGI AGGLAHPAAE RVLRSADLVV GIGATMGRST TQSMRLFADA QVVTVVSDAR
     GVAGVEPLLG DAVRTLEHTT ALARVATEPR EPWFHPVGPA AQCWAEDLRE FAPPIPDGTV
     DPRRAVARIS EHIPDDANVV ISNGHCSGFA AAFVTAPARG RFFAAQGFGS IGQALPTAIG
     VALGAPGRKT VVFEGDAAFM MHAQELDTAA RAGADLTVFV LNDQALGTEY QRLHLEGSDA
     GAAVVPTPGL AALAGALGAR ATTIDTDTAY AHAEAALRPG LAFVDVRTAR SVLSRHLRLP
     YRRVDPPQQV RSS
//
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