ID A0A410UUH2_9BURK Unreviewed; 335 AA.
AC A0A410UUH2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR006431};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR006431};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605, ECO:0000256|PIRNR:PIRNR006431};
GN ORFNames=EKL02_13020 {ECO:0000313|EMBL:QAU35027.1};
OS Janthinobacterium sp. 17J80-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2497863 {ECO:0000313|EMBL:QAU35027.1, ECO:0000313|Proteomes:UP000288813};
RN [1] {ECO:0000313|EMBL:QAU35027.1, ECO:0000313|Proteomes:UP000288813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J80-10 {ECO:0000313|EMBL:QAU35027.1,
RC ECO:0000313|Proteomes:UP000288813};
RA Kim M., Maeng S., Sathiyaraj S.;
RT "genome sequence of Janthinobacteria sp. 17J80-10.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585,
CC ECO:0000256|PIRNR:PIRNR006431};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006431}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR006431}.
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DR EMBL; CP035311; QAU35027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410UUH2; -.
DR KEGG; jaj:EKL02_13020; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000288813; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005944; Pro_iminopeptidase.
DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000313|EMBL:QAU35027.1};
KW Protease {ECO:0000256|PIRNR:PIRNR006431};
KW Reference proteome {ECO:0000313|Proteomes:UP000288813}.
FT DOMAIN 43..315
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 314
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 335 AA; 36773 MW; CC00CBDCAD38BFD9 CRC64;
MPINANSMPA HIRAPFCESH IAVGGGHRLY CAQYGEPGAP AAVVLHGGPG SGCKPAMLDW
FDLSRQRVVL LDQRGAGKSV PLGETAHNHT AHLVEDIEQV RVHLRIPRWL VVGGSWGATL
GLSYAGRYPA AVHGLVLRGA FLASAREVHR FFQSLQAEVP DAWARLTAGW SVAQQRNVLQ
SLTGLLQNGT CEQRNDAARR WHDYEEAIMR RMMASAAQTG QLANSRTVPG GLGSTPPESV
LAQTITKYRL QAHYLSQACF TSERALFRCA RRTAHIPTIL IHGTHDLVCP PENAQRLKRF
MPHADLRWVQ DGTHTPADPK VLAALRLAIR DVMQK
//
