ID   G2IN83_SPHSK            Unreviewed;       543 AA.
AC   G2IN83;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:BAK65531.1};
GN   ORFNames=SLG_08560 {ECO:0000313|EMBL:BAK65531.1};
OS   Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK65531.1, ECO:0000313|Proteomes:UP000001275};
RN   [1] {ECO:0000313|EMBL:BAK65531.1, ECO:0000313|Proteomes:UP000001275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6 {ECO:0000313|Proteomes:UP000001275};
RX   PubMed=22207743; DOI=10.1128/JB.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(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; AP012222; BAK65531.1; -; Genomic_DNA.
DR   RefSeq; WP_014075182.1; NC_015976.1.
DR   AlphaFoldDB; G2IN83; -.
DR   STRING; 627192.SLG_08560; -.
DR   KEGG; ssy:SLG_08560; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000001275; Chromosome.
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   CDD; cd02004; TPP_BZL_OCoD_HPCL; 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:SF13; 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   Reference proteome {ECO:0000313|Proteomes:UP000001275};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..107
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          183..316
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..530
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   543 AA;  58223 MW;  2A042E67BC25C67D CRC64;
     MKTCDAIVEI LKLEGVDVLF GYPRNALLEA AAQANIRTII PRQERIGLHM ADAYSRLTRG
     EKIGVFCCQH GPGAEVAYAG VAQAYGESVP ILVMPGGYST ATAHVGRNFN SVRNMAQITK
     SAEPLNFPSH VNAVMRRAFT ALRNGRGGPA LVELPFDVLE QDGAQVAYQP VLRSRFAPDG
     ESITRAASLL CAAKRPVLYA GQGIHWSGAY AELKELAELL AIPVCTSLPG KSSFDETHPL
     ALGSGGAAMP HAVRHFLDEA DVILGVGCSF TATAFGIRMP AGKTVIHATL DPVELNRAVE
     TDVALIGDAK LTLSALIAAC RALTGGAPRD MSAVTAEIRK LDDAWLAKWM PKLTSDQVPI
     TPYRVLWDLQ NTVDVANTII THDAGSPRDQ LSPFWKTRAP HSFLGWGKTT QLGYGLGLAM
     GAKLACPDKL CINVWGDAAI GFTGMDFETA VRERLPILSI LLNNASMAME LKVMPTATDR
     FRSTDISGNY AQFATALGGH GERISAVEDI VPAIRRAIAA TEAGKPALLE FMTSQEQEFS
     RYP
//