ID N0ANX5_9BACI Unreviewed; 376 AA.
AC N0ANX5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphonopyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B1NLA3E_03310 {ECO:0000313|EMBL:AGK52438.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK52438.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK52438.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK52438.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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DR EMBL; CP005586; AGK52438.1; -; Genomic_DNA.
DR RefSeq; WP_015592501.1; NC_021171.1.
DR AlphaFoldDB; N0ANX5; -.
DR STRING; 666686.B1NLA3E_03310; -.
DR KEGG; baci:B1NLA3E_03310; -.
DR eggNOG; COG0028; Bacteria.
DR eggNOG; COG4032; Bacteria.
DR HOGENOM; CLU_042853_0_0_9; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000013300; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0033980; F:phosphonopyruvate decarboxylase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000013300}.
FT DOMAIN 11..99
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 231..334
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 376 AA; 41449 MW; A2839311CECB8BB9 CRC64;
MINTSTLGGE LKALGFEVYS GVPCSYLKDL INYAINECEY VMATNEGEAV AVGAGASLGG
KKAVVLMQNS GLTNATSPLV SLTHPFQIPI LGFVSLRGEP GLPDEPQHEL MGRITAELLT
VLNIKWEYLS SEWGEVKRQL QRANHYIEQN QVFFFIVKKG TIDSVLLRKQ RLKKKTNLLM
RQKEMADQLP TRYEALRVIN SLKDHDTVQL ATTGKTGREL YELEDAANNL YMVGSMGCVS
SLGLGLSLTR PEKSIIAIDG DGALLMRMGN LATNGAYSPP NLLHILLDNQ THDSTGGQQT
VSDQIHFTEV AAACGYINAV YVHNLQELEE FIEGWKHDKC LTFLYLKISG GSKKGLGRPK
MKPSEVKERL QVFLDG
//
