ID A0A3G2JLL1_9ACTN Unreviewed; 563 AA.
AC A0A3G2JLL1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:AYN41212.1};
GN ORFNames=D9753_22635 {ECO:0000313|EMBL:AYN41212.1};
OS Streptomyces dangxiongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1442032 {ECO:0000313|EMBL:AYN41212.1, ECO:0000313|Proteomes:UP000268329};
RN [1] {ECO:0000313|EMBL:AYN41212.1, ECO:0000313|Proteomes:UP000268329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z022 {ECO:0000313|EMBL:AYN41212.1,
RC ECO:0000313|Proteomes:UP000268329};
RA Zhang B.;
RT "The genome of Streptomyces dangxiongensis Z022.";
RL Submitted (OCT-2018) 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; CP033073; AYN41212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G2JLL1; -.
DR KEGG; sdd:D9753_22635; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000268329; 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; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000268329};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 27..145
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 58702 MW; 7F758D41E1E8670A CRC64;
MTHDHDLVLR PTAAQTEAAL NPPAGRNGGD LVVETLAGLG ATTVFGLPGQ HALGMFDALR
RSTLHYVGLR VENNAGFAAD AYGRITGEAA PLLLSTGPGA LTSLAALQEA AAASAPVLAI
SSQIPTAGLG GGRHGYLHEL PDQAASFRGV VKSVHTVRTQ SQIPSAVAAA WKSALTAPHG
PVWVEIPQDV LLAETALPVV TAIDATPDDL VPRPELTAVA ADLLSNAARP VIIAGGGVVR
SDASGKLRRL AEKLDAPVVT TFGGKGAFPW KHPLSLQSWL EDRHTTDFLE DADVLLVVGS
GLGELSSNYH TFKPRGRVIQ IEADAGKLES NHPALGIHAD ARLALQALLE TVTERTDASA
PERVRNVLAR IEQRIASQEL TLEQDVLAAV RAALPADSPS FWDMTILAYW AWSAFDAQGP
NTMHSAQGAG GLGYGFPAAL GAATADPTRP VLAVSGDGGA LYSVAELATA RQYDLPVTWL
IVDDGGYGIL REYMTEAFGR TTATDLTGPD FVALAESFGV PGVRTTPESL KKDLTKALSA
PGPSVVVLPA VLRMFAPTHL GSD
//
