ID   DPAL_ECOL6              Reviewed;         398 AA.
AC   P66900; Q46804;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=c3449;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81894.1; -; Genomic_DNA.
DR   RefSeq; WP_000110493.1; NC_004431.1.
DR   AlphaFoldDB; P66900; -.
DR   SMR; P66900; -.
DR   STRING; 199310.c3449; -.
DR   EnsemblBacteria; AAN81894; AAN81894; c3449.
DR   GeneID; 66673256; -.
DR   KEGG; ecc:c3449; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021802_8_0_6; -.
DR   OMA; VMQGYTA; -.
DR   BioCyc; ECOL199310:C3449-MON; -.
DR   Proteomes; UP000001410; 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.
FT   CHAIN           1..398
FT                   /note="Diaminopropionate ammonia-lyase"
FT                   /id="PRO_0000185591"
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