ID M1WSK7_9NOST Unreviewed; 499 AA.
AC M1WSK7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=COG0028: Thiamine pyrophosphate-requiring enzymes {ECO:0000313|EMBL:CCH67514.1};
GN ORFNames=RINTHH_13590 {ECO:0000313|EMBL:CCH67514.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH67514.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH67514.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH67514.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) 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:CCH67514.1}.
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DR EMBL; CAIY01000044; CCH67514.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WSK7; -.
DR STRING; 1165094.RINTHH_13590; -.
DR Proteomes; UP000053051; 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; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000053051};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..64
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 134..267
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 326..474
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 499 AA; 54118 MW; 23C530DBC501F4F3 CRC64;
MADVYGRLTG KAGVCLSTLG PGATNLMTGV ADANLDSSPL VAITGQVGTD RMHIESHQYL
DLVAMFAPVT KWNKQIVRPS ITPEVVRKAF KKAQAEEPGA VHIDLPENIA AMPVKGEPLR
PDNNEKTYTS FAIIRAAAAA VSQATNPIIL VGNGAIRAQA SDAVTQFATQ MNIPVVNTFM
GKGVIPYTHP LALWSVGLQQ RDFINCGFDN TDLVIAIGYD LIEFSPKKWN PEGSIPIIHV
GLNKAEIDSS YIPLVEVVGD ISNSLTEIAK LADRDLKPNP YAISLKANIR ADYEQYANDN
GFPVKPQKLI HDLREVMGPD DVVISDVGAH KIWMARHYHC HSPNTCLISN GFAAMGIAIP
GALAAKLVYP NRKVVAVTGD GGFMMNCQEL ETALRVGTAF VTLIFHDGGY GLIGWKQENH
FGEGKSSFIE FGNPDFVKLA ESMGLKGYRV NASEDFIPIL KEALAQDVPA IIDCPVDYRE
NIRLTQKADK LSCMSQEST
//
