ID A0A0T5ZTA8_9BACT Unreviewed; 563 AA.
AC A0A0T5ZTA8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate domain-containing TPP-binding protein {ECO:0000313|EMBL:KRT65918.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KRT65918.1};
GN ORFNames=XU11_C0017G0044 {ECO:0000313|EMBL:KRT65918.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65918.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65918.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65918.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT65918.1}.
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DR EMBL; LDXN01000017; KRT65918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZTA8; -.
DR STRING; 1640508.XU11_C0017G0044; -.
DR PATRIC; fig|1640508.3.peg.1173; -.
DR Proteomes; UP000051780; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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; 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 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};
KW Transferase {ECO:0000313|EMBL:KRT65918.1}.
FT DOMAIN 6..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 61584 MW; 9712CDE05C90795D CRC64;
MAKVHGGWLV VRTLYELGVR EIFSLSGGHI NPIYDACVDF GIRIIDTHHE QAAAMAADAF
GRVKRQPGVC LVTAGPGFTN AVTGIAGAYL SNSPCLLLSG KSGIEENDRL PLQDIDQQSV
ITPITKWART IFDTKRIPEY ISTAYKKAIS GKPGPVYLGM PYEVLYESCN EEEIDRYNTI
IPSYKVEAAR EAIAQAVEML KSARRPVAIA GSGAWYSGAD KELIRILDKV KIPIFTLNFG
RGIVSDDHPL CFGAASPSAP VAFKRITSEA DLILLLGIRL SLYIGFGRTF NPEAKIIQVD
IDPGEIGRNR PADLGIVGDV SKVLSQLSDY VEKHSINLNY KSWVDQAKAW REDEWKKVEE
IRNSNKTPIH ALRVIKEVED VLGEDGMLAI DGGDTQVWTD TTYRVTKPGH YVKGGPLGCM
GVGVPFAIGT KVACPDKQVA LISGDGAIGM NFMEFETAIR HKIPFVTVVC NDQSWGMTKH
QLWITYGRER PTVGVDLPLI PFHEMVKVLG GYGELVTEPA QIHGALIRAF SSGVPALLNV
TTDPEAISPA TYALTQMMMP KKK
//
