ID A0A1V0AJG2_9ACTN Unreviewed; 311 AA.
AC A0A1V0AJG2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN ORFNames=BKM31_12985 {ECO:0000313|EMBL:AQZ70360.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ70360.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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; CP017717; AQZ70360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0AJG2; -.
DR STRING; 1909395.BKM31_12985; -.
DR KEGG; noa:BKM31_12985; -.
DR Proteomes; UP000190797; 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:UP000190797}.
FT DOMAIN 24..290
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 311 AA; 34495 MW; 84320A3C19671EFB CRC64;
MLDVGDGNLV YWEVCGNPDG KPAVVVHGGP GSGCSTGSRR RFDPERFRIV LFDQRNCGRS
RPHAGDPATD LSNNTTHHLI ADMELLREHL GIDKWLMYGG SWGSTLILAY AETHPERVSE
IVIPAVTMTR RSEIEWLYRG VGRFFPEAQE RFLQGVPEAD RDGDVFGVLA AYSRLLADPD
QKVREKAAQD WVTWEDAVIS QEVNGKPNAY SDRPADAVMA LTRICAHYFA NGAWLEEGVL
LRNAHRLAGI PGALIHGRMD MGGPLQTAWE LTRAWPDAEL HIVSDSGHTG SETFRKVLRE
AIERFSPAQP G
//
