ID A0A0Q8CNT1_9MICO Unreviewed; 591 AA.
AC A0A0Q8CNT1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KRA11925.1};
GN ORFNames=ASD61_07895 {ECO:0000313|EMBL:KRA11925.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA11925.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA11925.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11925.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA11925.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11925.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRA11925.1}.
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DR EMBL; LMGR01000001; KRA11925.1; -; Genomic_DNA.
DR RefSeq; WP_055820482.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CNT1; -.
DR STRING; 1736567.ASD61_07895; -.
DR Proteomes; UP000051073; 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; 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; 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:UP000051073};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
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 591 AA; 63049 MW; 871492F375899919 CRC64;
MSSGTVADVI VARLKEWGVQ RVFGYSGDGI NGLITALDRA GNEPQFFQAR HEENAAFMAV
GQAKFTGEAG VVISTQGPGA VHILNGLYDA KLDGVPVVAI VGQQKRSVLG AGYMQEVDLP
ALFADVAGYS QLVSSPEQVP FVIDRAFRTA LATQSPSVVI LPHDVQTAEA SEPSHEHGAI
NTEPEYRQPR VLPNDADLEA AAEVLSSGRK VAMLVGQGAR QAWPSVVALA ERLGAGVTCS
LLGKPVVDER LPFVAGTMGH LGTTASAFVL GACDTLLIIG SNDPWTEFYP APGQARAVQI
DIDGRFIGNR YPVEVGLVGD AALTLDALLP LITGEPDDSW SAEVTDAVSR WHRIREQRSQ
VPADPVNPEA VLAALNPRVP TDAQIGLDVG SVVYWYARQL TLPSGVTAHV SGTLASMGCS
LPYALAAKSA NPDRPTIVLT GDGGFQMTGV AELLTLSREW RRWSDPRFVI CVLANQDLAE
VTWEQREMET SPRFAASQEL PSFPAAEYAR LLGLDGETVS DPSQLASAWD RALASDRPYL
LEVITDPGVP LLPPFPAGEQ KLTGMFEALE AEGESGHHAA ELLRVYASHE R
//
