Tag | Content |
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CPLM ID | CPLM-000500 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphonoacetaldehyde hydrolase |
Protein Synonyms/Alias | Phosphonatase; Phosphonoacetaldehyde phosphonohydrolase |
Gene Name | phnX |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Bacillus cereus |
NCBI Taxa ID | 1396 |
Lysine Modification | Position | Peptide | Type | References |
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50 | RKPMGLLKIDHVRAL | acetylation | [1] | 118 | SLRERGIKIGSTTGY | acetylation | [1] | 143 | EAALQGYKPDFLVTP | acetylation | [1] | 189 | GDTVSDMKEGRNAGM | acetylation | [1] |
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Reference | [1] Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis. Zhang G, Mazurkie AS, Dunaway-Mariano D, Allen KN. Biochemistry. 2002 Nov 12;41(45):13370-7. [ PMID: 12416981] |
Functional Description | Involved in phosphonate degradation. |
Sequence Annotation | ACT_SITE 9 9 Nucleophile. ACT_SITE 50 50 Schiff-base intermediate with substrate. METAL 9 9 Magnesium. METAL 11 11 Magnesium; via carbonyl oxygen. METAL 183 183 Magnesium. |
Keyword | 3D-structure; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Schiff base. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 264 AA |
Protein Sequence | MKIEAVIFDW AGTTVDYGCF APLEVFMEIF HKRGVAITAE EARKPMGLLK IDHVRALTEM 60 PRIASEWNRV FRQLPTEADI QEMYEEFEEI LFAILPRYAS PINGVKEVIA SLRERGIKIG 120 STTGYTREMM DIVAKEAALQ GYKPDFLVTP DDVPAGRPYP WMCYKNAMEL GVYPMNHMIK 180 VGDTVSDMKE GRNAGMWTVG VILGSSELGL TEEEVENMDS VELREKIEVV RNRFVENGAH 240 FTIETMQELE SVMEHIEKQE LIIS 264 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0008967; F:phosphoglycolate phosphatase activity; IEA:InterPro. GO:0050194; F:phosphonoacetaldehyde hydrolase activity; IEA:HAMAP. GO:0019700; P:organic phosphonate catabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |