ASPA_PROMS
ID ASPA_PROMS Reviewed; 301 AA.
AC A2BP19;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable aspartoacylase {ECO:0000255|HAMAP-Rule:MF_00704};
DE EC=3.5.1.15 {ECO:0000255|HAMAP-Rule:MF_00704};
GN OrderedLocusNames=A9601_02421;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate;
CC Xref=Rhea:RHEA:10872, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58497; EC=3.5.1.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00704};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00704};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00704};
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00704}.
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DR EMBL; CP000551; ABM69530.1; -; Genomic_DNA.
DR RefSeq; WP_011817715.1; NC_008816.1.
DR AlphaFoldDB; A2BP19; -.
DR SMR; A2BP19; -.
DR STRING; 146891.A9601_02421; -.
DR EnsemblBacteria; ABM69530; ABM69530; A9601_02421.
DR KEGG; pmb:A9601_02421; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_083292_0_0_3; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 632656at2; -.
DR Proteomes; UP000002590; Chromosome.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..301
FT /note="Probable aspartoacylase"
FT /id="PRO_1000147941"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 61..62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ SEQUENCE 301 AA; 34646 MW; 8EA38ABA6744DED3 CRC64;
MTVQRILIVS GTHGNEINPV WAVKQFNREE NSLKHGIEYE YIIGNPVAYE KGCRYIDVDL
NRSFKESENC DQQKNSFYET NRANFLLDEF GIDGSKPCQI VIDLHTTTAN MGTSIVLYGR
RFKDFCLAAL LQNKFGLPIY LHEKDKAQTG FLVEAWPCGL VIEIGAVAQN FYDPKIIDRF
SLIISSLREE IDKLKNNLIE LPKELVVYVH QGSIDYPRDK KGVIDGLIHP ERINQDWKMI
KKGDPLFLDS QGIVHKYDGD QLIWPVFIGE VAYKEKNIAM SYTKKEVICS KKQWVQDFES
L
