(data stored in ACNUC7421 zone)

SWISSPROT: A8FPZ3_SHESH

ID   A8FPZ3_SHESH            Unreviewed;       317 AA.
AC   A8FPZ3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
DE            Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE            EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431};
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN   OrderedLocusNames=Ssed_0303 {ECO:0000313|EMBL:ABV34916.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34916.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34916.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34916.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide.
CC       {ECO:0000256|PIRNR:PIRNR006431}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006431}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|PIRNR:PIRNR006431}.
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DR   EMBL; CP000821; ABV34916.1; -; Genomic_DNA.
DR   RefSeq; WP_012004442.1; NC_009831.1.
DR   ProteinModelPortal; A8FPZ3; -.
DR   STRING; 425104.Ssed_0303; -.
DR   ESTHER; shesh-a8fpz3; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; ABV34916; ABV34916; Ssed_0303.
DR   KEGG; sse:Ssed_0303; -.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000171480; -.
DR   KO; K01259; -.
DR   OMA; YDLLCPP; -.
DR   OrthoDB; POG091H04PE; -.
DR   BioCyc; SSED425104:GH7Q-312-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPZ3.
DR   SWISS-2DPAGE; A8FPZ3.
KW   Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000313|EMBL:ABV34916.1};
KW   Protease {ECO:0000256|PIRNR:PIRNR006431}.
FT   DOMAIN       34    274       AB hydrolase-1 (Alpha/Beta hydrolase fold
FT                                1). {ECO:0000259|Pfam:PF00561}.
FT   ACT_SITE    108    108       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
FT   ACT_SITE    260    260       {ECO:0000256|PIRSR:PIRSR006431-1}.
FT   ACT_SITE    290    290       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
SQ   SEQUENCE   317 AA;  35508 MW;  12E2967EAAEC1732 CRC64;
     MSSHLPAFIR RDWLDVGDGH VLHLAQHGNP DGIPLLFLHG GPGGGCAVED LRLFDRDTFH
     IFLLDQRGAG RSKPHGELKH NDLLHLLGDI ERVRLWLNIP AWCVVGGSFG ATLGFIYSCL
     YPQRVLSQVL WGLFIPNEEG ANWLYGNQGA ATLFPQDYLE FTALAPFSAK IDTLFKRYQS
     GFLDPDVDTR LEYVRGWLKW ELALALPGAE LPESGTPLAK SLAEIELHYA SQQYFGAYAL
     MREMACGIKA DTVILQGEMD WVCPSVIVEK FLEEFGSGDM KYTLIKGGYH ALANDKMFLE
     VVYAVQEMAN NMREIDK
//

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