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Database: UniProt
Entry: B9NWE2_9RHOB
LinkDB: B9NWE2_9RHOB
Original site: B9NWE2_9RHOB 
ID   B9NWE2_9RHOB            Unreviewed;       190 AA.
AC   B9NWE2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:EEE35616.1};
DE            EC=4.1.1.82 {ECO:0000313|EMBL:EEE35616.1};
GN   ORFNames=RKLH11_3216 {ECO:0000313|EMBL:EEE35616.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE35616.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/jb.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT   Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL   J. Bacteriol. 193:5011-5012(2011).
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DR   EMBL; DS999532; EEE35616.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9NWE2; -.
DR   STRING; 467661.RKLH11_3216; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_117492_1_0_5; -.
DR   OrthoDB; 9773408at2; -.
DR   Proteomes; UP000005135; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EEE35616.1};
KW   Pyruvate {ECO:0000313|EMBL:EEE35616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          38..157
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   190 AA;  20492 MW;  2BD775F35D9F53B7 CRC64;
     MIIDRDAALS ALIPHVAERD IVVAVYQSCF DWLQLNPRDL NYVAVGAMGQ ASSHGLGLAL
     ANPDRRVIIL DGDGSLLMNL GALVTIANAG VTNLYHFLAA NRVYEVNGAH PLPGADRVDF
     VGFARSAGYA GSQSFGELDL FTEALPYILA APGPQFVSME VRPGQSYPRD YDYIHSAQAR
     QTFRAALNRG
//
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