ID B2IUF9_NOSP7 Unreviewed; 294 AA.
AC B2IUF9;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=Probable aspartoacylase;
DE EC=3.5.1.15;
GN OrderedLocusNames=Npun_R2728;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M.,
RA Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: N-acyl-L-aspartate + H(2)O = a carboxylate +
CC L-aspartate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase
CC subfamily.
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DR EMBL; CP001037; ACC81265.1; -; Genomic_DNA.
DR RefSeq; YP_001866208.1; NC_010628.1.
DR ProteinModelPortal; B2IUF9; -.
DR STRING; 63737.Npun_R2728; -.
DR EnsemblBacteria; ACC81265; ACC81265; Npun_R2728.
DR GeneID; 6252113; -.
DR KEGG; npu:Npun_R2728; -.
DR PATRIC; 22758016; VBINosPun48114_3197.
DR eggNOG; COG2988; -.
DR HOGENOM; HOG000232489; -.
DR KO; K01437; -.
DR OMA; WPIFINE; -.
DR ProtClustDB; PRK02259; -.
DR BioCyc; NPUN63737:GJNP-2637-MONOMER; -.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:HAMAP.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR HAMAP; MF_00704; Aspartoacylase; 1; -.
DR InterPro; IPR016708; Aspartoacylase.
DR InterPro; IPR007036; Aste_AspA.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF018001; Aspartoacylase; 1.
PE 3: Inferred from homology;
KW Complete proteome; Hydrolase; Metal-binding; Zinc.
FT REGION 63 64 Substrate binding (By similarity).
FT METAL 14 14 Zinc (By similarity).
FT METAL 17 17 Zinc (By similarity).
FT METAL 106 106 Zinc (By similarity).
FT BINDING 56 56 Substrate (By similarity).
FT BINDING 166 166 Substrate (By similarity).
FT BINDING 277 277 Substrate (By similarity).
SQ SEQUENCE 294 AA; 33119 MW; D6A5434B09590647 CRC64;
MNQINRVAIV GGTHGNEFTG AYLIEKFAQF PDLITRQSFE TVTLLANPNA FAAGRRYVEK
DLNRCFLKQD LQNPTLNSYE ELQAKSIQNT LGSNRNKQAD FILDLHSSTA NMGLTIILVN
SHPLNLQLAA YLSQISPLVR IYRCSFKSIT ENPFVNSLCE LGFAIEVGPI AQGILKATLF
QQTEELVYAV LDYLEQFNQG KIASTNETLI LYDHLSVVDY PKQQDGKIFA MIHPELQDKD
YQALNPGDPM FITFDNKTIV YEGASTVWPI FINEAAYYEK GIAMCLTQKQ QINI
//
