ID A0A0Q5QYW2_9SPHN Unreviewed; 549 AA.
AC A0A0Q5QYW2;
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:KQS04387.1};
GN ORFNames=ASG11_09105 {ECO:0000313|EMBL:KQS04387.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS04387.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS04387.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04387.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS04387.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04387.1,
RC ECO:0000313|Proteomes:UP000051080};
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:KQS04387.1}.
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DR EMBL; LMPM01000001; KQS04387.1; -; Genomic_DNA.
DR RefSeq; WP_055778022.1; NZ_LMPM01000001.1.
DR AlphaFoldDB; A0A0Q5QYW2; -.
DR STRING; 1736350.ASG11_09105; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051080; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Reference proteome {ECO:0000313|Proteomes:UP000051080};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 549 AA; 58345 MW; F084E5AF7FDD2395 CRC64;
MTENRTGGRI LVDQLVAQGC DRIFTVPGES FLAVLDALHD TPEIDLVVCR QEGGVGFMAC
ADGAMTGRPG IAFVTRGPGA TNASIGVHVA MQDSQPMILF IGDVDRATKD REAFQEVDFT
AMFAPLCKWA AKIDDARRIP EYIARAFATA MNGRPGPVVL ALPEDMLLDA VEAVDRPRVN
RVEQDALIEA ASTANDMLKA AKRPVAIIGG AGWTPHTAAA VAAFGEQSGV PLVAAFRRQD
AVPNNCPVYA GNLGYGPNPK LAARVRDADL LIVIGARLGE ATTDGYTLVT PDHPGQSLIH
IHPDPAELNS TFRADLAICA DAERFANLME MLAAEQTPIA AGAEAHAEYL AWSTPAPRDL
MLDLGPCVAA MREKLPADSI ICNGAGNYSG WWHRYWRYAG PTSQLAPTAG AMGYGVPAAT
AAALRYPDRT VVALAGDGCF LMNGQELATA VAHGASMLVL VIDNGWYGTI RMHQEREFPG
RVTGTRLLNP DFAALGRAYG CWAETVETTA EFVPALDRAM AKTGVRLLHL KTDVEAITAG
TTLTKVRGG
//
