ID A3YVT2_9SYNE Unreviewed; 312 AA.
AC A3YVT2;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Probable aspartoacylase {ECO:0000256|HAMAP-Rule:MF_00704};
DE EC=3.5.1.15 {ECO:0000256|HAMAP-Rule:MF_00704};
GN ORFNames=WH5701_15546 {ECO:0000313|EMBL:EAQ76234.1};
OS Synechococcus sp. WH 5701.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76234.1, ECO:0000313|Proteomes:UP000002935};
RN [1] {ECO:0000313|EMBL:EAQ76234.1, ECO:0000313|Proteomes:UP000002935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00704};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00704,
CC ECO:0000256|PIRSR:PIRSR018001-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00704,
CC ECO:0000256|PIRSR:PIRSR018001-3};
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000256|ARBA:ARBA00006173, ECO:0000256|HAMAP-Rule:MF_00704}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ76234.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANO01000002; EAQ76234.1; -; Genomic_DNA.
DR RefSeq; WP_006172037.1; NZ_CH724159.1.
DR AlphaFoldDB; A3YVT2; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_083292_0_0_3; -.
DR OrthoDB; 531770at2; -.
DR Proteomes; UP000002935; Unassembled WGS sequence.
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 CDD; cd06909; M14_ASPA; 1.
DR Gene3D; 2.20.25.160; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00704; Aspartoacylase; 1.
DR InterPro; IPR016708; Aspartoacylase.
DR InterPro; IPR007036; Aste_AspA.
DR PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF018001; Aspartoacylase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00704};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00704}; Reference proteome {ECO:0000313|Proteomes:UP000002935};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00704}.
FT ACT_SITE 163
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 62..63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
SQ SEQUENCE 312 AA; 33437 MW; E6FF17ACB152372B CRC64;
MGAAAVLVVA GTHGNERNAP WLLEHWLAHP GALDAAGLAL QLVIGNPGAL AAGRRYLDRD
LNRSFTSALL EAPGPADREV QRARELLALH GPAGSRPCAL VLDLHSTTAA MGNSLVVYGR
RPVDLALAAG IQALLGLPIY LHEADASQQG FLLECWPCGL VIEVGPVPQG VVNAAICHQT
QRALEAALAV LASARRGDLA LPRGLTVHRH LGSLDLPRHP DGRPAACLHP LRQHRDWQVI
RPGDPLFVTA GGETLRYEPT DPEPLWPVFI NEAAYGEKGI ALSLTRRERW PCEAAWAEDL
QQLAKHLTLS TG
//
