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Database: UniProt
Entry: A0A0Q9N0H0_9MICC
LinkDB: A0A0Q9N0H0_9MICC
Original site: A0A0Q9N0H0_9MICC 
ID   A0A0Q9N0H0_9MICC        Unreviewed;       562 AA.
AC   A0A0Q9N0H0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KRE71665.1};
GN   ORFNames=ASG77_11650 {ECO:0000313|EMBL:KRE71665.1};
OS   Arthrobacter sp. Soil762.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE71665.1, ECO:0000313|Proteomes:UP000051715};
RN   [1] {ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE71665.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE71665.1,
RC   ECO:0000313|Proteomes:UP000051715};
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   -!- 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:KRE71665.1}.
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DR   EMBL; LMSG01000019; KRE71665.1; -; Genomic_DNA.
DR   RefSeq; WP_056346959.1; NZ_LMSG01000019.1.
DR   AlphaFoldDB; A0A0Q9N0H0; -.
DR   OrthoDB; 3203527at2; -.
DR   Proteomes; UP000051715; 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; 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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          186..310
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          386..518
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   562 AA;  57828 MW;  589B748B04EA5602 CRC64;
     MTTLTVSGRV AQVLSSYLSD VFGVMGNGNV YFLDAAEKLG LRFSPVRHEG AAIAAADAYY
     RASGRLAAGT TTYGPGYTNA LTALAEAVQA QIPVVLVTGD APSSGARPQD VDQAAIAAGL
     GAATFTVTRE AAGSITQQAV EYALTKRTAV VIAIPYDLAA LEAADEELPA PLAPQVTDDV
     DGGLGQVARL LAGAKRPLIL AGRGAHLAGA GPELRELADR LGALTAGTAL ALNLLQGDGY
     LGVAGGFGTD TAAGLMGEAD VVLVAGASLS PFTMRFGHLL GPDSTVIQID AALQPTHPRV
     DTFVSADVKS AAGRILRMLD GPASPDANLT DASRAEAWRA EARRRLAEGP AHHPGSDETA
     DGRLDPRSLA KALDAVLPER RTVVQDGGHF VGWAPMYWRI PRPQDLVMVG TAYQAIGLGL
     ASAVGAARSV EDGRTLVLAS GDGGFLMGLS DLESLIGAAS SAVVVIYNDA AYGAEIHQYG
     SQGLTQKPML IPEVDFSGIA RALGAESAII RSLTDLSALT DWIDAGAKGT FVADCRITSS
     VRAPWLSEWM QAKQEAKAAV AG
//
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