(data stored in ACNUC29543 zone)

SWISSPROT: A5GQV1_SYNR3

ID   A5GQV1_SYNR3            Unreviewed;       308 AA.
AC   A5GQV1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=SynRCC307_0357 {ECO:0000313|EMBL:CAK27260.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27260.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27260.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00704, ECO:0000256|PIRSR:PIRSR018001-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00704, ECO:0000256|PIRSR:PIRSR018001-3};
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00704}.
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DR   EMBL; CT978603; CAK27260.1; -; Genomic_DNA.
DR   RefSeq; WP_011934775.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0357; -.
DR   EnsemblBacteria; CAK27260; CAK27260; SynRCC307_0357.
DR   KEGG; syr:SynRCC307_0357; -.
DR   eggNOG; ENOG4108Q6X; Bacteria.
DR   eggNOG; COG2988; LUCA.
DR   HOGENOM; HOG000232489; -.
DR   KO; K01437; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 632656at2; -.
DR   BioCyc; SSP316278:G1GJL-353-MONOMER; -.
DR   Proteomes; UP000001115; 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   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;
DR   PRODOM; A5GQV1.
DR   SWISS-2DPAGE; A5GQV1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00704,
KW   ECO:0000256|SAAS:SAAS00453982, ECO:0000313|EMBL:CAK27260.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00704,
KW   ECO:0000256|PIRSR:PIRSR018001-3, ECO:0000256|SAAS:SAAS00454002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00704, ECO:0000256|PIRSR:PIRSR018001-
KW   3, ECO:0000256|SAAS:SAAS00074961}.
FT   REGION       61     62       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00704}.
FT   ACT_SITE    164    164       {ECO:0000256|PIRSR:PIRSR018001-1}.
FT   METAL        12     12       Zinc. {ECO:0000256|HAMAP-Rule:MF_00704,
FT                                ECO:0000256|PIRSR:PIRSR018001-3}.
FT   METAL        15     15       Zinc. {ECO:0000256|HAMAP-Rule:MF_00704,
FT                                ECO:0000256|PIRSR:PIRSR018001-3}.
FT   METAL       106    106       Zinc. {ECO:0000256|HAMAP-Rule:MF_00704,
FT                                ECO:0000256|PIRSR:PIRSR018001-3}.
FT   BINDING      54     54       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00704}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00704}.
FT   BINDING     274    274       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00704}.
SQ   SEQUENCE   308 AA;  33643 MW;  AD00CE8D2F5CFEA1 CRC64;
     MVASVLVVGG THGNECNAPW LLQQWGPSFA ALQRPRLKVQ TALGNPRALQ CCRRYIDRDL
     NRSFRGDLLQ AQPSPADQWE VQRARELVQS FGPQGTKPCQ VVIDLHSTTA AMGNSLVVYG
     RRPADLALAA ACQERLGLPI YQHEHDPDQT GFMAEAWPCG LVLEVGPVPQ GVISPVICQQ
     TQLGLETLLD LLDEASQGHL QLRSPLRVHR HSGSLDLPRD SSGQPTSCLH PARLKSDWTP
     LKPGAPLFQQ GDGTVIPFSG EPDQVTVFSN EAAYQEKHIA TSLARRVSIP CDPSWSRALS
     DLLQGVDH
//

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