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
//