ID F8GGD7_NITSI Unreviewed; 576 AA.
AC F8GGD7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:AEJ02411.1};
GN OrderedLocusNames=Nit79A3_2644 {ECO:0000313|EMBL:AEJ02411.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02411.1};
RN [1] {ECO:0000313|EMBL:AEJ02411.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02411.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002876; AEJ02411.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GGD7; -.
DR STRING; 261292.Nit79A3_2644; -.
DR KEGG; nii:Nit79A3_2644; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_4; -.
DR OrthoDB; 2254214at2; -.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..317
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 576 AA; 62673 MW; 730F2E100722F825 CRC64;
MGRTVAEQLV EMLKAAGIRR IYGVTGDSLN FFNDALRRDG SIDWIHVRHE EVGAYAAMAE
GVLGGMGCCA GSSGPGHVHL INGLYDAHRW GSPVLALAST ITSEDYGTES FQSTDLHMFD
GCSHYNEVAT TPQQLPRMLQ QALQHAWNRK GVGVCAFPGD LMTCNAEENA LCADLYRPQP
VMIPSDTEIQ LLAELINSSE DIGIYAGVGC ADARVEVIEL ARLLKAPMAY TLKAKMMLEY
DNPYAVGLTG LLGNKAGARA ITGGKLLLML GSDFPWKEFL DSSIKIVQID TKPERLGRRV
ALHMGLCGDI GPTLRNLLPL INPKVKDVFL NACLADYAEV EEDHRVHAAD PGEENLIKPE
FVAAMIDRLA DDDAIFTADT GMSTVWAARY LHGSGKRTLM GSFSHGSMAN AMPQSIGAAL
HSPERQVIAF CGDGGISMLM GDLMTIAQYK LPIKLIVFNN HSLGMVELEM QVAGLPDWQT
KMINPDFAMV AEACGIRGYS VTNPDKLENT LQEALLHNGP ALVDVFTNPH VPTLPPHTSI
GVMSRYIQSQ AKLALGGRMD EAWDAFRTNI KYIRDL
//
