ID   A0A0Q8RLG1_9SPHN        Unreviewed;       555 AA.
AC   A0A0Q8RLG1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE22_01465 {ECO:0000313|EMBL:KRB94638.1};
OS   Sphingomonas sp. Root720.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB94638.1, ECO:0000313|Proteomes:UP000051570};
RN   [1] {ECO:0000313|EMBL:KRB94638.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|EMBL:KRB94638.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB94638.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|EMBL:KRB94638.1};
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KRB94638.1}.
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DR   EMBL; LMID01000001; KRB94638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8RLG1; -.
DR   STRING; 1736595.ASE22_01465; -.
DR   Proteomes; UP000051570; 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; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051570};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..99
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          186..317
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..531
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   555 AA;  60360 MW;  C49DCFB0FC2CAC6B CRC64;
     MKVGAAIAEI LKREGVEYIF GYPVNMITEF AADADIRSII ARSERVAGHM ADAMSRVSSG
     ENIGVYFMQH GPGIENGMGA VAQAFGESVP ILVIPMGYAR NEAWVEPNFN SSVSLRSFSK
     SVEPVVSGKH LPDVMRRAFS RLRSGRGGPV VVEVPIDMWD EEVPEPLRYT PVRKVRSGPD
     PDAIVEAADM LLAAERPVIY AGQGIHYAKA WPQLCCLAET LGAPVTTSLE GKSAFDETHP
     LSLGSGGLAL PRTVRHFLDN ADVIFGVGCS FTKTLFGVPM PRGKRFIHAT LDPAHFDNEV
     PVTIGILGDA ALTLDALIAE IDRRLDGKAR DWSAVVEEID MVRAEWMAAW APKLTSDETP
     ITPYRVIGDL MKTVDVANTV ITHDAGSPRD QLSPFWRAVT PLGYLGWGKT TQLGYGLGLA
     MGAKVAHPDK LCINLWGDAA IGFTGMDFET CVRERIPILS ILFNNFSMAM ETHIMKRSHE
     KFGTIDISGD YAAMARAFGG YGERVTDPAE IVPALRRAIA QTEAGVPVLL EFITCKELAT
     SKETQRYAQA ERPAN
//