PHNXW_CLOD6
ID PHNXW_CLOD6 Reviewed; 636 AA.
AC Q183T0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Bifunctional phosphonoacetaldehyde hydrolase/aminoethylphosphonate transaminase;
DE Includes:
DE RecName: Full=Phosphonoacetaldehyde hydrolase;
DE Short=Phosphonatase;
DE EC=3.11.1.1;
DE AltName: Full=Phosphonoacetaldehyde phosphonohydrolase;
DE Includes:
DE RecName: Full=2-aminoethylphosphonate--pyruvate transaminase;
DE EC=2.6.1.37;
DE AltName: Full=2-aminoethylphosphonate aminotransferase;
DE AltName: Full=AEP transaminase;
DE Short=AEPT;
GN Name=phnXW; OrderedLocusNames=CD630_28490;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- FUNCTION: Involved in phosphonate degradation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2-aminoethyl)phosphonate + pyruvate = L-alanine +
CC phosphonoacetaldehyde; Xref=Rhea:RHEA:17021, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57418, ChEBI:CHEBI:57972, ChEBI:CHEBI:58383; EC=2.6.1.37;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate;
CC Xref=Rhea:RHEA:18905, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58383; EC=3.11.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HAD-like
CC hydrolase superfamily. PhnX family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-V
CC pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180355; CAJ69737.1; -; Genomic_DNA.
DR RefSeq; WP_011861713.1; NZ_CP010905.2.
DR RefSeq; YP_001089362.1; NC_009089.1.
DR AlphaFoldDB; Q183T0; -.
DR SMR; Q183T0; -.
DR STRING; 272563.CD630_28490; -.
DR PRIDE; Q183T0; -.
DR EnsemblBacteria; CAJ69737; CAJ69737; CD630_28490.
DR KEGG; cdf:CD630_28490; -.
DR KEGG; pdc:CDIF630_03116; -.
DR PATRIC; fig|272563.120.peg.3001; -.
DR eggNOG; COG0075; Bacteria.
DR eggNOG; COG0637; Bacteria.
DR OMA; IREMCEM; -.
DR PhylomeDB; Q183T0; -.
DR BioCyc; PDIF272563:G12WB-3009-MON; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0047304; F:2-aminoethylphosphonate-pyruvate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro.
DR CDD; cd02586; HAD_PHN; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01376; PhnW_aminotrans_5; 1.
DR HAMAP; MF_01375; PhnX; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR012703; NH2EtPonate_pyrv_transaminase.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006323; Phosphonoacetald_hydro.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR03301; PhnW-AepZ; 1.
DR TIGRFAMs; TIGR01422; phosphonatase; 1.
DR TIGRFAMs; TIGR02326; transamin_PhnW; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Pyridoxal phosphate; Pyruvate; Reference proteome;
KW Schiff base; Transferase.
FT CHAIN 1..636
FT /note="Bifunctional phosphonoacetaldehyde
FT hydrolase/aminoethylphosphonate transaminase"
FT /id="PRO_0000284607"
FT REGION 1..276
FT /note="Phosphonoacetaldehyde hydrolase"
FT REGION 277..636
FT /note="2-aminoethylphosphonate--pyruvate transaminase"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 56
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 465
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 636 AA; 72044 MW; 368B79C8BE2A4E8E CRC64;
MKKIYGEKIK AVVFDWAGTT VDYGCFAPLN VFIEIFKRRG IDVTMEEARK PMGKLKIDHI
REMCEMDRIK NIWSDKFGKV PTEDDVNELY AEFEPMLFET LEEYTTPIPH VVETIEKLRK
NGLKIGSTTG YTREMMNIVE PNAAKKGYSP DFLVTPSEVS QGRPYPWMCY KNAEALGVSP
MSSMVKVGDT ISDVKEGVNA GMWSVAVIKG SSELGLTQEE VENMDKEELK AKMSIVSKKF
KEAGAHFVIE TMAELEDILI KIENETIKSD FVPENDYILL TPGPLSTTKS VRASMLKDWC
TWDVEYNNLV QDVRRRLVSL ATQNTDKYTS VLMQGSGTFS VEAIIGSTIS KDGKLLVIAN
GAYGKRMKDI CNYLNIQFVD CTFKDIEAVD LNVVENLLKE NKDITHISMV HCETTTGRLN
PIQEVGKLAK EYNKIYIVDA MSSFGGIEID VEDFNIDFLV SSSNKCIQGV PGFGFIIANK
EELSKCKGIA KSLSLDVYAQ WDTMEKNNGK WRFTSPTHVV RAFYQALLEL EEEGSVEKRY
ARYKENQFTI ASRLKSLGFD TLVNDNAQSP VITTFLYPKN AKFEFMEFYT YLKDNGFVIY
PGKLTDIDTF RIGSIGEVYP TDMERLADVI EKFINR
