ID F5YHL4_TREPZ Unreviewed; 373 AA.
AC F5YHL4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:AEF86847.1};
DE EC=4.1.1.82 {ECO:0000313|EMBL:AEF86847.1};
GN Name=aepY {ECO:0000313|EMBL:AEF86847.1};
GN OrderedLocusNames=TREPR_2365 {ECO:0000313|EMBL:AEF86847.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86847.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86847.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF86847.1; -; Genomic_DNA.
DR RefSeq; WP_015707839.1; NC_015578.1.
DR AlphaFoldDB; F5YHL4; -.
DR STRING; 545694.TREPR_2365; -.
DR KEGG; tpi:TREPR_2365; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_042853_1_0_12; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
DR CDD; cd03371; TPP_PpyrDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR017684; Phosphono-pyrv_decarboxylase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03297; Ppyr-DeCO2ase; 1.
DR PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AEF86847.1};
KW Pyruvate {ECO:0000313|EMBL:AEF86847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT DOMAIN 4..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 231..343
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 373 AA; 40619 MW; B9DF6DE7FF18DEA5 CRC64;
MIEAQLFYDI LSEKGTGFFT GVPDSLLKSF CAYITDHAGY NSHIIAVNEG AALALASGYH
IASGKIPLVY MQNSGIGNAI NPLLSLADAD VYRIPMLLLI GWRGEPGVKD EPQHLKQGKV
TLSLLEAMGI PYFILSQNEG EFRQQIDQCF ASIKEKNTPH ALVIRKDTFA PYTLVKKEAD
EGELTREAAI EEVIRASDPE EIYFSTTGMA SRELYEIRER LGQGHGRDFL TVGSMGHASQ
IALGAALQKP NQPITVLDGD GALLMHMGAL AAIGNRKPEH FRHIILNNGA HDSVGGQPTL
GLKIDIPSIA RACGYRESCT VKSAEELRAV LGQKRHGPVL IEIRVRKGAR KDLGRPASSP
QENKKVLMGI LND
//
