ID A0A1F8MXM7_9CHLR Unreviewed; 412 AA.
AC A0A1F8MXM7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Thiamine pyrophosphate enzyme TPP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A2Y91_00355 {ECO:0000313|EMBL:OGO03356.1};
OS Chloroflexi bacterium RBG_13_54_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797630 {ECO:0000313|EMBL:OGO03356.1, ECO:0000313|Proteomes:UP000180313};
RN [1] {ECO:0000313|EMBL:OGO03356.1, ECO:0000313|Proteomes:UP000180313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGO03356.1}.
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DR EMBL; MGMX01000121; OGO03356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MXM7; -.
DR Proteomes; UP000180313; 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 Gene3D; 3.40.50.970; -; 1.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
FT DOMAIN 31..160
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 241..374
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 412
FT /evidence="ECO:0000313|EMBL:OGO03356.1"
SQ SEQUENCE 412 AA; 45465 MW; 1B2D9F4A37FAF0D1 CRC64;
MSVRDERELQ GEIPLAAVAP DSPTLGDPKS VEKAVRMLLE AKRPFIAAGE GVHWADASSE
LQELAELLNV PVHSRRIARG AVPEDHPLAV RAGYRARFWT DCDVIAIIGL HLGGLEGLGL
PPVWPAKAKR IIIHESAEDA WQPLPVALKI IGNAKMVLRQ MIDCAKSIIK ERPKRTEWLE
WLDKCQREHA EWQSEALAEY VDHKPVHAVK LAQDIVDFLD DSATIVYDAF CGTSFLTDRV
KAKFSGQILD TGTWGGVGHG VGMGIGAQLA RPGKQVLVLM GDGGIGVGGM DIETASRYKL
PVVYVICNNS TWLAGSYMAF FKNQVYPWDM LPDIRYDKMF EPVGCHGENV TDPKDIIPAL
KRAFNSGKTS VVNVLMDSRV FNPWLGSWGM TIVAKLSADV TKCPEDWQDF LM
//
