ID A0A0K2GHN4_NITMO Unreviewed; 545 AA.
AC A0A0K2GHN4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thiamine pyrophosphate enzyme, central domain family {ECO:0000313|EMBL:ALA60431.1};
GN ORFNames=NITMOv2_4047 {ECO:0000313|EMBL:ALA60431.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA60431.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA60431.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA60431.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP011801; ALA60431.1; -; Genomic_DNA.
DR RefSeq; WP_053381292.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GHN4; -.
DR STRING; 42253.NITMOv2_4047; -.
DR KEGG; nmv:NITMOv2_4047; -.
DR PATRIC; fig|42253.5.peg.3995; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000069205; Chromosome.
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:UP000069205};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 59257 MW; 777D104741BA1A38 CRC64;
MRAADLLIRC LEHEGVQWLF GVPGEETLEI TDAVLNSSLR FITTRHEQGA AFMADVYGRL
TGRAGVCLST LGPGATNLIT GVADANLDHA PLVAISGQVS TERKHSQSHQ YIDLPALFKP
ITKWNGVIAT PAMIPETVRK AFKLAETEKP GAVHLEIPED VAAERVDESA VVPPLRVQSP
RVPEPSAVQV ARAVAVLRGA KRPLILAGNG VVRRRAEEAV RRFARRLQIP VVHTFMGKGV
MPDTDPLSLY TIGFPGRDYA ARMVEQADVV IAVGYDFVEY APCLWNPNRD KRLVHVDVSP
ADVDAHYIVE VGVLGDLAQA LDRLAEGVAP FEARWAEGAR AAVGAQLEEE GAGPAGWPLR
PQRIITELRD VLPADALVIC DVGAHKLWMA RMFPCYAPNT CLISNGFAAM GIALPGAVAA
QLLYPSRRIV AVTGDGGFMM NSQELETAVR LQLPLVILIW RDGGYGVIRW KQTLRFNRAS
SVEFGNPDFV AYARAYGAQG YRVEGPTELT PILREALRSG GPAVIDCPVD YGENVRVTDR
LKRIP
//
