ID Q2NAA0_ERYLH Unreviewed; 325 AA.
AC Q2NAA0;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 105.
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|PIRNR:PIRNR006431};
GN OrderedLocusNames=ELI_06495 {ECO:0000313|EMBL:ABC63391.1};
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC63391.1, ECO:0000313|Proteomes:UP000008808};
RN [1] {ECO:0000313|Proteomes:UP000008808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX PubMed=19168610; DOI=10.1128/JB.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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, ECO:0000256|RuleBase:RU003421};
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,
CC ECO:0000256|RuleBase:RU003421}.
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DR EMBL; CP000157; ABC63391.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2NAA0; -.
DR STRING; 314225.ELI_06495; -.
DR ESTHER; 9sphn-q2naa0; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR KEGG; eli:ELI_06495; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_5; -.
DR OMA; FYQDGAS; -.
DR Proteomes; UP000008808; 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 NCBIfam; TIGR01249; pro_imino_pep_1; 1.
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 ECO:0000256|RuleBase:RU003421}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Protease {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Reference proteome {ECO:0000313|Proteomes:UP000008808}.
FT DOMAIN 47..305
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 325 AA; 36486 MW; 5165678881BE57ED CRC64;
MANSNMLDYK RTLYPEIEPY ETGMLDVGEG HQLYYERVGT PGAKPAVFLH GGPGGGMAPS
HRRQWDPELY DVLLFDQRGC GKSLPFAEIE HNDTWRIVAD IERLREMCGH EAWQVFGGSW
GATLALAYAQ KHPERTTEIV LRGVFLARQN EKSWLYQYGA SEIMAEQWDE FSGHIPEAER
DDLVQAYYAR LTSDDEPTRL AAAKQWSLWE GTVATLLPNA DLLADFEDPA KAVPFARICA
RFFLENFYLE EGQLLRDMQS IGHIPTIIVQ GRHDICTPPG AAWAVKKAHP AAELWMVHDA
GHSASEPGIV DGLVRATDQF ADKSK
//