ID D0I617_GRIHO Unreviewed; 296 AA.
AC D0I617;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Probable aspartoacylase {ECO:0000313|EMBL:EEY73331.1};
DE EC=3.5.1.15 {ECO:0000313|EMBL:EEY73331.1};
GN ORFNames=VHA_001184 {ECO:0000313|EMBL:EEY73331.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY73331.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY73331.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY73331.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR018001-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR018001-3};
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000256|ARBA:ARBA00006173}.
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:EEY73331.1}.
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DR EMBL; ADAQ01000010; EEY73331.1; -; Genomic_DNA.
DR RefSeq; WP_005502804.1; NZ_ADAQ01000010.1.
DR AlphaFoldDB; D0I617; -.
DR GeneID; 58894475; -.
DR eggNOG; COG2988; Bacteria.
DR OrthoDB; 531770at2; -.
DR Proteomes; UP000003604; Unassembled WGS sequence.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0000313|EMBL:EEY73331.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR018001-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000003604};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT ACT_SITE 166
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
SQ SEQUENCE 296 AA; 33342 MW; 8D3C5E337E74F660 CRC64;
MNTFNRVAIV GGTHGNEFSG IYLLRKWQDT PALISRPSFE TETLFANPNA FRDNKRYIDC
DLNRQFAPAD LDNPSLGNYE QSRAKAINQQ LGPKGNARTD LIIDLHNTTS NMGPTLILLK
NDAFNTQLAA YVSERMENAV ILFEDHCSMD EQLFLCSIAN QGIIVEVGPQ PQSVVRQDVL
EWMDSMTGHI LDFVDLYNKG EVPELPDTIS AYRYVETLKL PENAQGERIG MVHKSVQDAD
FTPLNNGDPI FTTFDGSEIY WNGNYEAYPH FINEAAYYDN NLAMSLGKKV DITVIK
//
