1A1D_PSEPU
ID 1A1D_PSEPU Reviewed; 338 AA.
AC Q5PWZ8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACC deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACCD {ECO:0000255|HAMAP-Rule:MF_00807};
DE EC=3.5.99.7 {ECO:0000255|HAMAP-Rule:MF_00807};
GN Name=acdS {ECO:0000255|HAMAP-Rule:MF_00807};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UW4;
RX PubMed=9851025; DOI=10.1139/w98-074;
RA Shah S., Li J., Moffatt B.A., Glick B.R.;
RT "Isolation and characterization of ACC deaminase genes from two different
RT plant growth-promoting rhizobacteria.";
RL Can. J. Microbiol. 44:833-843(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-44.
RC STRAIN=UW4;
RX PubMed=15588698; DOI=10.1016/j.bbapap.2004.09.015;
RA Hontzeas N., Zoidakis J., Glick B.R., Abu-Omar M.M.;
RT "Expression and characterization of 1-aminocyclopropane-1-carboxylate
RT deaminase from the rhizobacterium Pseudomonas putida UW4: a key enzyme in
RT bacterial plant growth promotion.";
RL Biochim. Biophys. Acta 1703:11-19(2004).
CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen
CC source. {ECO:0000255|HAMAP-Rule:MF_00807, ECO:0000269|PubMed:15588698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00807,
CC ECO:0000269|PubMed:15588698};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00807};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for 1-aminocyclopropane-1-carboxylate
CC {ECO:0000269|PubMed:15588698};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15588698};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC -!- CAUTION: Was originally (PubMed:9851025) thought to originate from
CC Pseudomonas sp. Then it was changed to Enterobacter cloacae, then to
CC P.putida. {ECO:0000305|PubMed:9851025}.
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DR EMBL; AF047710; AAD05069.1; -; Genomic_DNA.
DR EMBL; AY823987; AAV73804.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5PWZ8; -.
DR SMR; Q5PWZ8; -.
DR BRENDA; 3.5.99.7; 5092.
DR SABIO-RK; Q5PWZ8; -.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00807; ACC_deaminase; 1.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005965; ACP_carboxylate_deaminase.
DR InterPro; IPR020601; ACP_carboxylate_deaminase_bac.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01274; ACC_deam; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..338
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_0000184502"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT MUTAGEN 44
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15588698"
FT CONFLICT 177..179
FT /note="EEV -> KEL (in Ref. 1; AAD05069)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="E -> D (in Ref. 1; AAD05069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36874 MW; B4827E8BEF82C2AE CRC64;
MNLNRFERYP LTFGPSPITP LKRLSEHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP
EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR
IMGADVRLDA AGFDIGIRPS WEKAMSDVVE RGGKPFPIPA GCSEHPYGGL GFVGFAEEVR
QQEKELGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GVDASAKPEQ TKAQILRIAR
HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH
GMIEMVRRGE FPDGSKVLYA HLGGAPALNA YSFLFRNG
