ID M1YX62_NITG3 Unreviewed; 549 AA.
AC M1YX62;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein {ECO:0000313|EMBL:CCQ90258.1};
GN ORFNames=NITGR_270018 {ECO:0000313|EMBL:CCQ90258.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ90258.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ90258.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ90258.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(2013).
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:CCQ90258.1}.
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DR EMBL; CAQJ01000030; CCQ90258.1; -; Genomic_DNA.
DR RefSeq; WP_005007610.1; NZ_HG422173.1.
DR AlphaFoldDB; M1YX62; -.
DR STRING; 1266370.NITGR_270018; -.
DR HOGENOM; CLU_013748_3_2_0; -.
DR InParanoid; M1YX62; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000011704; 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; 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:UP000011704};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 549 AA; 60779 MW; 083ADDAB99D4CF1B CRC64;
MKASDLFVRS LEQEGVEAIF GVPGEETLNL MESLRHSNIQ FILTRHEQAA GFMAATYGRL
TGRVGVCLST LGPGVTNLVT AGAYAQLGAM PMLMISGQKP IKKSKQGRFQ IVDAIAMMRP
LTKSTRQVVH GNSIPVIVRE SVRLAQEERP GAVHIELPED IAEEECASQP YPVQAVRRPH
ADELAIEQAA GMLMQAKRPL VLIGAGANRY RTSQALKQFV DHTGIYFFNT QMGKGVVDER
HPKFLGTAAL SHKDYLHCAI EQADLILNVG HDVIEKPPFF MHASGATQVI HVNFFSSNVD
EVYFPQLDVV GDIADSIERL REQVSPAAHW DFSFFEKVKQ ELEQHIEEKA AQQRFPVGPE
YLVGEIRHIM PDDGILALDN GLYKIWFARN YKAYGLNTLL LDNALASMGA GLPSAMAARM
VFPDRKVMAI CGDGGFMMNA QELETAVRLK LDLVVVVLCD NAYGMIKWKQ TGLGFPAFGM
DYTNPDFCQF AEAHGATGHR VKRAEELSKV LKECLDTPGL HLVEVPIDYS EDEKDLIEEI
KTKTAALQK
//
