ID A0A2H3L3M0_9CHLR Unreviewed; 569 AA.
AC A0A2H3L3M0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:PDV97745.1};
GN ORFNames=A9Q02_17800 {ECO:0000313|EMBL:PDV97745.1};
OS Candidatus Chloroploca asiatica.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Candidatus Chloroploca.
OX NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV97745.1, ECO:0000313|Proteomes:UP000220922};
RN [1] {ECO:0000313|EMBL:PDV97745.1, ECO:0000313|Proteomes:UP000220922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7-9 {ECO:0000313|EMBL:PDV97745.1,
RC ECO:0000313|Proteomes:UP000220922};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:PDV97745.1}.
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DR EMBL; LYXE01000126; PDV97745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3L3M0; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000220922; 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; cd02002; TPP_BFDC; 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:UP000220922};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..551
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 569 AA; 60996 MW; A2782F8BC9E59125 CRC64;
MRKRTGNQAI IEQFLADGMN FMFGNPGTVE QGFLDAVADY PEMRYILTLQ ESVAVMAADG
YARATQRPTL VQMHSSPGLG NAIGALYQAK RGHSPLVVIG GDAGLRYMNT ESQMYGDLVA
FAEPVTKWST MVLEPANLLR VIRRAIKIAA TPPMGPVYVC VPADVLDAPA VEPVMPTSLF
STRVAPAGAM IAEMAQMLVS AATPIIFVGD GVAYSGAQAE LTRVAELLGA EVWEADSGEV
NMAYDHPLYQ GMTGHMFGFA SKPITQKGDV NLICGTYMLP EVFPELGPIF AEGAKVIHID
LDPGAIAKNH PVDLGVLADP KLTLGLLAEA IDASFSSEQR AAAQARAATI GQRNAEKRAS
QLQADQAVRE ATPLKMSRFM EELVAQLPSE DVIIVDEALT SSPALVRYWP PQRTGAYFLT
RGGSLGIGFP GAIGAKLANP SKTVLGFSGD GGSMYTIQSL WSAARHNLDV KFIVCNNSSY
RLLQLNIDQY WKDQGLPKRD YPLSFDLSSP PLGFVDMARG MGVAGIRIEK PEEVAGAIKQ
MLDHPGPFLI DLALEGDVHP ERVGATCGQ
//
