DPAL_SALTY
ID DPAL_SALTY Reviewed; 404 AA.
AC P40817;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Diaminopropionate ammonia-lyase;
DE Short=DAPAL;
DE EC=4.3.1.15 {ECO:0000269|PubMed:3275662};
DE AltName: Full=2,3-diaminopropionate ammonia-lyase;
DE AltName: Full=Alpha,beta-diaminopropionate ammonia-lyase;
DE AltName: Full=Diaminopropionatase;
GN Name=dpaL; OrderedLocusNames=STM1002;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-22; 67-88 AND 239-242, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATES, AND SUBUNIT.
RC STRAIN=IFO 12529;
RX PubMed=3275662; DOI=10.1016/s0021-9258(19)35446-8;
RA Nagasawa T., Tanizawa K., Satoda T., Yamada H.;
RT "Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification
RT and characterization of the crystalline enzyme, and sequence determination
RT of the pyridoxal 5'-phosphate binding peptide.";
RL J. Biol. Chem. 263:958-964(1988).
RN [3]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=IFO 12529;
RX PubMed=12821154; DOI=10.1016/s0006-291x(03)01100-8;
RA Khan F., Jala V.R., Rao N.A., Savithri H.S.;
RT "Characterization of recombinant diaminopropionate ammonia-lyase from
RT Escherichia coli and Salmonella typhimurium.";
RL Biochem. Biophys. Res. Commun. 306:1083-1088(2003).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=22904288; DOI=10.1128/jb.01362-12;
RA Kalyani J.N., Ramachandra N., Kachroo A.H., Mahadevan S., Savithri H.S.;
RT "Functional analysis of the genes encoding diaminopropionate ammonia lyase
RT in Escherichia coli and Salmonella enterica serovar Typhimurium.";
RL J. Bacteriol. 194:5604-5612(2012).
CC -!- FUNCTION: Catalyzes the alpha,beta-elimination reaction of both L- and
CC D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In
CC vitro L- and D-isomers of serine are also degraded, though slowly; it
CC is the only serine dehydratase which can eliminate an amino group at
CC the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow
CC growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit
CC enzymes involved in the synthesis of pyruvate and aspartate, as well as
CC amino acids derived from them. {ECO:0000269|PubMed:12821154,
CC ECO:0000269|PubMed:22904288, ECO:0000269|PubMed:3275662}.
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:0000269|PubMed:3275662};
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:0000269|PubMed:3275662};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12821154, ECO:0000269|PubMed:3275662};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:12821154, ECO:0000269|PubMed:3275662};
CC -!- ACTIVITY REGULATION: Competitively inhibited by L- and D-alanine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=852 umol/min/mg enzyme for L-DAP {ECO:0000269|PubMed:3275662};
CC Vmax=447 umol/min/mg enzyme for D-DAP {ECO:0000269|PubMed:3275662};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:3275662};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12821154,
CC ECO:0000269|PubMed:3275662}.
CC -!- INDUCTION: By DL-DAP (at protein level). {ECO:0000269|PubMed:22904288}.
CC -!- DISRUPTION PHENOTYPE: No growth on minimal medium plus DL-DAP; growth
CC can be restored by a mix of 8 amino acids (Arg, Asn, Cys, Glu, Ile,
CC Leu, Met and Thr). {ECO:0000269|PubMed:22904288}.
CC -!- SIMILARITY: Belongs to the diaminopropionate ammonia-lyase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL19936.1; -; Genomic_DNA.
DR RefSeq; NP_459977.1; NC_003197.2.
DR RefSeq; WP_000544849.1; NC_003197.2.
DR PDB; 5YGR; X-ray; 2.50 A; A/B/C/D=1-404.
DR PDBsum; 5YGR; -.
DR AlphaFoldDB; P40817; -.
DR SMR; P40817; -.
DR STRING; 99287.STM1002; -.
DR PaxDb; P40817; -.
DR PRIDE; P40817; -.
DR EnsemblBacteria; AAL19936; AAL19936; STM1002.
DR GeneID; 1252520; -.
DR KEGG; stm:STM1002; -.
DR PATRIC; fig|99287.12.peg.1058; -.
DR HOGENOM; CLU_021802_8_0_6; -.
DR OMA; VMQGYTA; -.
DR PhylomeDB; P40817; -.
DR BioCyc; SENT99287:STM1002-MON; -.
DR BRENDA; 4.3.1.15; 2169.
DR SABIO-RK; P40817; -.
DR Proteomes; UP000001014; 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; -; 3.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..404
FT /note="Diaminopropionate ammonia-lyase"
FT /id="PRO_0000185593"
FT MOD_RES 78
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT CONFLICT 16
FT /note="Y -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="F -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:5YGR"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 202..223
FT /evidence="ECO:0007829|PDB:5YGR"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5YGR"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:5YGR"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:5YGR"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:5YGR"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:5YGR"
SQ SEQUENCE 404 AA; 44152 MW; 9D605DFEAA691F00 CRC64;
MHELIKYQFN TRRKKYGTGA ALSLLNGNVG HEVLAFHKKL PNYAVTPLHN LAHLSQRLGL
GSIHIKDESW RFGLNAFKGL GGSYAVGKYL ADKLQCDINS LSFAALNTPE IKEKIKDCVF
VTATDGNHGR GVAWAAEQLG LKAVVYMPKG SSLIRAENIR HHGAECTITD LNYDDAVRLA
HRMAQTKGWV LLQDTAWTGY EEIPTWIMQG YMTLAVEAYE QLAETNSPLP THLILQAGVG
SFAGSVMGYF VEKMQENIPN IIVVEPHQAN CLYQSAVMDD GQPHCVTGDM ATIMAGLACG
EPNIISWPII RDNTSCFISA DDCLAAKGMR ISAAPRPGTD TPFISGESGA IGVGLLYELM
NNMHYQDLAN RLQLDASAHV LLISTEGDTS PDIYEDIVWN GRSA
