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Database: UniProt
Entry: A0A010YQ44_9ACTN
LinkDB: A0A010YQ44_9ACTN
Original site: A0A010YQ44_9ACTN 
ID   A0A010YQ44_9ACTN        Unreviewed;       574 AA.
AC   A0A010YQ44;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Thiamine pyrophosphate-dependent enzyme, putative carboligase or decarboxylase {ECO:0000313|EMBL:EXG82295.1};
GN   ORFNames=CryarDRAFT_3461 {ECO:0000313|EMBL:EXG82295.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG82295.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG82295.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG82295.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXG82295.1}.
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DR   EMBL; JFBT01000001; EXG82295.1; -; Genomic_DNA.
DR   RefSeq; WP_035851984.1; NZ_KK073874.1.
DR   AlphaFoldDB; A0A010YQ44; -.
DR   PATRIC; fig|927661.3.peg.3422; -.
DR   HOGENOM; CLU_013748_3_1_11; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000021053; Unassembled WGS sequence.
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: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   Ligase {ECO:0000313|EMBL:EXG82295.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          397..550
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  61093 MW;  CD6B3AF434E7CDA6 CRC64;
     MTTTAAAALT AQLESYGVEY VFGTCGHTNI ALLDALGRSS IEFVIARHEQ AAAHAADGYA
     RASGKPGVVL LHVGPGMMNA VTGVATAALD SVPLIAIAGD IPSYYHGRHP HQEVNLHNDA
     DQTAIYRPFV KRAWHVQRVE DLPRFTERAF TTAVSGRPGA VLLDVPMDLF SRPQTAESYP
     MPGELTRPDL PEGTAERIAD ALVAAERPLI YVGGGLSAGP GREALTALVE HLDIPVAHSL
     MAKGSLPDDH PLVMGMPGFW GLEETNRYAR EADVVLAIAT RFAETDASSW NDRYTWSFPP
     TRLIQIDIDP AELGRNFPVE IGAVADAALA MRRIAAAALR RPEASRPALR ESITAARGAL
     FAGSAERGRS DDFPLRPERI LLDLRETLPA DTVLVTDVGW NKNGVAQAYP LPVEGRFITP
     GGASTMGFGP AAALGVQIAW PDRPVVALIG DGGMSAQLPA LPMAVERGLP VLFVVMNNQA
     HGTIADLQAA NFGAGYGCEF TDADGNPYSP DFAALGQACG ADGYRIEEPG DLRKALHAAL
     ANRRPAVLDV PMVNEPVPTP GHWNIKDIYA GIFE
//
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