ID B7K3E1_RIPO1 Unreviewed; 289 AA.
AC B7K3E1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Probable aspartoacylase {ECO:0000256|HAMAP-Rule:MF_00704};
DE EC=3.5.1.15 {ECO:0000256|HAMAP-Rule:MF_00704};
GN OrderedLocusNames=PCC8801_0363 {ECO:0000313|EMBL:ACK64461.1};
OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS 8801)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK64461.1, ECO:0000313|Proteomes:UP000008204};
RN [1] {ECO:0000313|Proteomes:UP000008204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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}.
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DR EMBL; CP001287; ACK64461.1; -; Genomic_DNA.
DR RefSeq; WP_012593738.1; NC_011726.1.
DR AlphaFoldDB; B7K3E1; -.
DR STRING; 41431.PCC8801_0363; -.
DR KEGG; cyp:PCC8801_0363; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_083292_0_0_3; -.
DR OrthoDB; 531770at2; -.
DR Proteomes; UP000008204; 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 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:UP000008204};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00704}.
FT ACT_SITE 162
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 15
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 18
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 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 64..65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 104
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 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
SQ SEQUENCE 289 AA; 33300 MW; EA3A2143330D35A7 CRC64;
MVKKIRNIAL IGGTHGNEMT GVYLIKKFQK YPHLIERSSL KILTFLANPR AIEARQRYIE
TDLNRCFSRE ALDEPETFFY EQILAKNIDQ KIRDHQTDLI IDLHSTTSQM GLTIIICDGH
PFHFQLVAYL TSLNPNIKVL RYRYAQENLL LRSLTELGFA IEVGAVAQGV LDAALFQQTE
QLIYHLLDGL EKYNQGDDFN GCKSLTLYQV IERIDYPRTG EDITAMIHPD LQFKDYHPLH
PGDPLFVTFE GETIHYQGDC TVYPVFINEA AYYEKGIAMC FTEKQEIIL
//