ID F5XMH0_MICPN Unreviewed; 318 AA.
AC F5XMH0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 Name=pip {ECO:0000313|EMBL:BAK36427.1};
GN OrderedLocusNames=MLP_34130 {ECO:0000313|EMBL:BAK36427.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK36427.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK36427.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) 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, 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; AP012204; BAK36427.1; -; Genomic_DNA.
DR RefSeq; WP_013864286.1; NC_015635.1.
DR AlphaFoldDB; F5XMH0; -.
DR STRING; 1032480.MLP_34130; -.
DR MEROPS; S33.001; -.
DR KEGG; mph:MLP_34130; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_043739_2_2_11; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000007947; 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; PR00111; ABHYDROLASE.
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:UP000007947}.
FT DOMAIN 35..299
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 298
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 318 AA; 34774 MW; 8144C87E1E47DDED CRC64;
MRAGYPPIEP YASGLLDVGD GQQIYWEECG SPAGKPVVFL HGGPGGGSNP GVRRLFDPAR
YRIVLLDQRG CGRSRPHASE TGDLSTNTTW HLVADLERLR EARGIERWQV FGGSWGSALA
LAYAESHPER VTELVLRGIF TLRRSELDFY YNGGAGQLFP DRYETFLGPL GGRDFRGDAI
AAYHDLLFDP DPAVHGPAAV AWSTWEAATI TLLPDEELIA SFAEPSYALA FARIENHYFV
HGGWFAEGQL IADAGRLRDI PGVIVQGRYD VATPAVTAWD LHWAWPTAEF CLIDDAGHAY
SERGITAALV AATDRFAG
//
