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Database: UniProt
Entry: I1D122_9PSEU
LinkDB: I1D122_9PSEU
Original site: I1D122_9PSEU 
ID   I1D122_9PSEU            Unreviewed;       583 AA.
AC   I1D122;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:EIE98646.1};
GN   ORFNames=SacglDRAFT_01735 {ECO:0000313|EMBL:EIE98646.1};
OS   Saccharomonospora glauca K62.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE98646.1, ECO:0000313|Proteomes:UP000005087};
RN   [1] {ECO:0000313|EMBL:EIE98646.1, ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|EMBL:EIE98646.1,
RC   ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT   K62.";
RL   Submitted (JAN-2012) 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; CM001484; EIE98646.1; -; Genomic_DNA.
DR   RefSeq; WP_005463540.1; NZ_CM001484.1.
DR   AlphaFoldDB; I1D122; -.
DR   STRING; 928724.SacglDRAFT_01735; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_4_0_11; -.
DR   OrthoDB; 2443624at2; -.
DR   Proteomes; UP000005087; 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; cd02002; TPP_BFDC; 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:SF164; PYRUVATE DECARBOXYLASE; 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:EIE98646.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005087};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          16..146
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          221..329
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          430..577
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   583 AA;  62576 MW;  F4B095AE94442DEF CRC64;
     MGSDETSPQT AATGYTTSKA FLEALAEGGV RYVFANLGSD HPGILEAYAQ ARVEGREHAF
     PELVICPHES VAMAAALGYA QVTGVPQAVM VHVECGTQNI GGMLHNAAKG RIGVLMYAGA
     SPFTQEGELF GSRNEFIQWI QDVHDQRGIV RGYTKYDNEI RTGANVKQLV HRALQIARSA
     PAGPVYLVGP REVMESEAPT RQADAAHFPP VAPAALAPDV VDRVASALAE ARRPVVVTSY
     LGRDREAVPA LVELCEAAGA GVLESVPSYV NFPADHPLHW GFQWNDQHHN PLLEEADVVL
     VLGSDVPWIP TKNRPNAEAR VFVVDEDPLK DQMPLWHVPA ELFARADLGT AVRQLHHRVA
     ELADPAVVAR RRELAAAEHE RLWAERARRE TPVGETITPE YLVACVRDAI DDDTLVLTEA
     ITHYPTVSWH LHRTVPGSLL GSGAGSLGWA IGAAVGAKLA EPERTVVSLV GDGSYLFGVP
     SSVFWMARRY GAPSLTVVFD NKGWNAPKAS TLGVHPKGTA AQRDDFGVHF TDRPDLPGIA
     EAAGGAWGRT VEAASELKDA LAEALAAVRA GRPAVLAVRV PEM
//
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