ID C3XBF9_OXAFO Unreviewed; 575 AA.
AC C3XBF9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Thiamine pyrophosphate enzyme, N-terminal TPP binding domain protein {ECO:0000313|EMBL:EEO30535.1};
GN ORFNames=OFBG_01563 {ECO:0000313|EMBL:EEO30535.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO30535.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO30535.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO30535.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG658170; EEO30535.1; -; Genomic_DNA.
DR RefSeq; WP_005881775.1; NZ_GG658170.1.
DR AlphaFoldDB; C3XBF9; -.
DR STRING; 847.BRW83_0530; -.
DR GeneID; 77134440; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_4; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000005089; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000005089};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 62210 MW; 05805BB276FDF0A4 CRC64;
MGTTAEDSLN PETISGGHLV AKALRNEGVD TIFTLSGGNI VDIYDGCVSE GIRIIDFRHE
QVAAHAADGY ARQTGQTGCL VTTAGPGCCN AVIGLATALR SETPLLHIGG QGATTQYLQG
SLQEYDHVKL MSPVTKWASS VKTTERVADM VSMACREATG EVPGPVYLEV PRDILDKSVE
FKSCTIPAAG HYRCSPKVMC APEEIEKLAD LLIHAEKPAV LFGSQVWNSR SHVEAAEMVK
AFDIPAYTNG SARGILKSDN PHSFDRTRSM ALASADVILV VGTPFDFRLG YGKQLNPEAR
VVQIDQNYVE IGKNRDIELG LLGHAGTIFN AVIQSASGRV EKGARAKRRQ WMQELRVAEE
KALEKLMPLF HSENRLINPY RVAYELNEFL NDDTVYIGDG GDVVTISAQA VRPHNPGQWM
DPGPLGSLGV GTGFAIAAKL AHPEKEVLCY YGDGAFSMTA FDMETANRFN APYLAVVGNN
SAMNQIRYAQ LAKYGDRGNV GNLLSDLPYG KFAEMMGGYG EEVHNPEDIA GALQRGREAV
AKTGKCAVIN IWVDPQEWSP GTKARLKSRM VTAGK
//