ID   DPAL_ECO57              Reviewed;         398 AA.
AC   P66901; Q46804;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Diaminopropionate ammonia-lyase;
DE            Short=DAPAL;
DE            EC=4.3.1.15 {ECO:0000250|UniProtKB:P66899};
DE   AltName: Full=2,3-diaminopropionate ammonia-lyase;
DE   AltName: Full=Alpha,beta-diaminopropionate ammonia-lyase;
GN   Name=ygeX; OrderedLocusNames=Z4210, ECs3744;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the alpha,beta-elimination reaction of both L- and
CC       D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. The
CC       D-isomer of serine is degraded to pyruvate, though very poorly; other
CC       amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine)
CC       are not substrates. {ECO:0000250|UniProtKB:P66899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:22084, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57721; EC=4.3.1.15;
CC         Evidence={ECO:0000250|UniProtKB:P66899};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2,3-diaminopropanoate + H(+) + H2O = 2 NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:52432, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:136599;
CC         EC=4.3.1.15; Evidence={ECO:0000250|UniProtKB:P66899};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P66899};
CC       Note=Binds 1 pyridoxal phosphate per subunit.
CC       {ECO:0000250|UniProtKB:P66899};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P66899}.
CC   -!- SIMILARITY: Belongs to the diaminopropionate ammonia-lyase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG58000.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37167.1; -; Genomic_DNA.
DR   PIR; D85942; D85942.
DR   PIR; H91096; H91096.
DR   RefSeq; NP_311771.1; NC_002695.1.
DR   RefSeq; WP_000110493.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P66901; -.
DR   SMR; P66901; -.
DR   STRING; 155864.EDL933_4072; -.
DR   EnsemblBacteria; AAG58000; AAG58000; Z4210.
DR   EnsemblBacteria; BAB37167; BAB37167; ECs_3744.
DR   GeneID; 66673256; -.
DR   GeneID; 916434; -.
DR   KEGG; ece:Z4210; -.
DR   KEGG; ecs:ECs_3744; -.
DR   PATRIC; fig|386585.9.peg.3906; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021802_8_0_6; -.
DR   OMA; VMQGYTA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008838; F:diaminopropionate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR010081; DiNH2opropionate_NH3_lyase.
DR   InterPro; IPR019871; DiNH2propionate_NH3-lyase_sub.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR03528; 2_3_DAP_am_ly; 1.
DR   TIGRFAMs; TIGR01747; diampropi_NH3ly; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Diaminopropionate ammonia-lyase"
FT                   /id="PRO_0000185592"
FT   MOD_RES         77
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  43328 MW;  FAF1277E86D60232 CRC64;
     MSVFSLKIDI ADNKFFNGET SPLFSQSQAK LARQFHQKIA GYRPTPLCAL DDLANLFGVK
     KILVKDESKR FGLNAFKMLG GAYAIAQLLC EKYHLDIETL SFEHLKNAIG EKMTFATTTD
     GNHGRGVAWA AQQLGQNAVI YMPKGSAQER VDAILNLGAE CIVTDMNYDD TVRLTMQHAQ
     QHGWEVVQDT AWEGYTKIPT WIMQGYATLA DEAVEQMREM GVTPTHVLLQ AGVGAMAGGV
     LGYLVDVYSP QNLHSIIVEP DKADCIYRSG VKGDIVNVGG DMATIMAGLA CGEPNPLGWE
     ILRNCATQFI SCQDSVAALG MRVLGNPYGN DPRIISGESG AVGLGVLAAV HYHPQRQSLM
     EKLALNKDAV VLVISTEGDT DVKHYREVVW EGKHAVAP