ID A0A0S4LGH7_9BACT Unreviewed; 377 AA.
AC A0A0S4LGH7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:CUS35051.1};
DE EC=4.1.1.82 {ECO:0000313|EMBL:CUS35051.1};
GN Name=ppd {ECO:0000313|EMBL:CUS35051.1};
GN ORFNames=COMA1_20099 {ECO:0000313|EMBL:CUS35051.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS35051.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS35051.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS35051.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CZQA01000008; CUS35051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LGH7; -.
DR STRING; 1742972.COMA1_20099; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000199032; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CUS35051.1};
KW Pyruvate {ECO:0000313|EMBL:CUS35051.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199032}.
FT DOMAIN 7..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..345
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 377 AA; 40776 MW; 82FEE9C963D7BD29 CRC64;
MIDPQEFVAC LRANGVGFFS GVPDSLLKEL CSCIAQESSA DQHIVAANEG GAVALALGYH
LATGNIPLVY FQNSGLGNSI NPLLSLADQE VYAIPMLLVI GWRGEPGVHD EPQHKKQGRV
MLPMLDAMEI PFSLLSPELD RADTTLKDAV AHARTSSTPY ALVVKKDTFK PFTAFQPESP
SFPLSREEAI HQVIEGLDDR DVIVSTTGMP SREVYDYRRK KGSGHHRDFL TVGGMGHASH
IALGIALQQP DRSVYCLDGD GATLMHMGAL SLNGTLKAKN FKHIILNNGA HDSVGGQPTV
GLAIDFLSIA RASGYRQVLR AQTKQELASG LTDLKRSSGP SLLEIRVRRG ARKDLGRPAT
TPIQNKQAFM DFVRSQG
//
