ID A0A0K9XL68_9ACTN Unreviewed; 606 AA.
AC A0A0K9XL68;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KNB54080.1};
GN ORFNames=AC230_05990 {ECO:0000313|EMBL:KNB54080.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB54080.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KNB54080.1}.
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DR EMBL; LFXA01000002; KNB54080.1; -; Genomic_DNA.
DR RefSeq; WP_049714822.1; NZ_LFXA01000002.1.
DR AlphaFoldDB; A0A0K9XL68; -.
DR STRING; 1678637.AC230_05990; -.
DR PATRIC; fig|1678637.3.peg.1297; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000037288; Unassembled WGS sequence.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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:UP000037288};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 606 AA; 65591 MW; 604DC76689C9F9ED CRC64;
MSAKVSDHLL QRLREWGVER VFAYPGDGIN GLLAAWGRAD DNPRFIQARH EEMAAFEAVG
YAKFSGRVGV CAATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTNRSAMGG SYQQEVDLLS
LFKDVAADFC EMVTVPEQLP NVLDRALRTA VARRTVTALV IPADVQELDY TPPQHAFKMV
PSSLGAPVYA PVPADEEIAR AAEVVNEGKK VAVLIGQGAR AARAEVERLA DQVGAGVAKA
LLGKDALPDD LPYVTGAIGL LGTRPSYEMM RDCDTLVVIG SSFPYTQFMP EFGQARAVQI
DIDPFMVGLR YPFEVNLVGD AKETLARLLP RLKPKEHGDW RAGIEKNVAR WWEVMERRAA
VGAEPLNPEY VIHALDPLLP ADAVVTADSG SSANWYARHL RLRGTMRGSL SGTLATMGPG
VPYAIGAKFA HPERPAIALV GDGAMQMNGM AELITAAKYY REWQDPRLVV AVLNNRDLNQ
VTWEMRAMSG APQFLPSQEI PDVPYADVAR SFGLDGVRVE KHDDVVKAWA QALAADRPFV
LDFRTDPAVP PIPPHASLDQ IEAATSAVLK GDSDRAAMVR QGFKAKIQEM LPGGPRHHKS
GGGKGR
//