ID J4WCV0_9FIRM Unreviewed; 297 AA.
AC J4WCV0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR005539};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR005539};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR005539};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605, ECO:0000256|PIRNR:PIRNR005539};
GN Name=pepI {ECO:0000313|EMBL:EJU23306.1};
GN ORFNames=HMPREF1152_1006 {ECO:0000313|EMBL:EJU23306.1};
OS Mogibacterium sp. CM50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU23306.1, ECO:0000313|Proteomes:UP000003142};
RN [1] {ECO:0000313|EMBL:EJU23306.1, ECO:0000313|Proteomes:UP000003142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM50 {ECO:0000313|EMBL:EJU23306.1,
RC ECO:0000313|Proteomes:UP000003142};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC {ECO:0000256|PIRNR:PIRNR005539}.
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:PIRNR005539};
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJU23306.1}.
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DR EMBL; ALNL01000009; EJU23306.1; -; Genomic_DNA.
DR RefSeq; WP_009643218.1; NZ_ALNL01000009.1.
DR AlphaFoldDB; J4WCV0; -.
DR STRING; 936375.HMPREF1152_1006; -.
DR PATRIC; fig|936375.3.peg.109; -.
DR eggNOG; COG2267; Bacteria.
DR OrthoDB; 53505at2; -.
DR Proteomes; UP000003142; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; IPR005945; Pro_imino_pep.
DR NCBIfam; TIGR01250; pro_imino_pep_2; 1.
DR PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF5; PIMELOYL-[ACYL-CARRIER PROTEIN] METHYL ESTER ESTERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR005539,
KW ECO:0000313|EMBL:EJU23306.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539, ECO:0000313|EMBL:EJU23306.1};
KW Protease {ECO:0000256|PIRNR:PIRNR005539};
KW Reference proteome {ECO:0000313|Proteomes:UP000003142}.
FT DOMAIN 31..172
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 274
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 297 AA; 33806 MW; C43DC68159AD16F7 CRC64;
MAKVTEGYMP FLDYRTYYRI VGEKKDNGKA PLICLHGGPG STHNYYEVLD NVADDDERQI
IMYDQLGCGN SYLDGHPELW TQDTWLDELE ALREHLGLDE CHIIGQSWGG MMQIAYAIER
APKGVKSFVI SSGHPSSSLW EKEGLRRIKM MPQDMQDAIN HALETGDFTG EAYDRAVAEY
MHRYCDYWIG ADAPECCTRP KKTGGEAYLY GWGPNEFAPT GSLRDFEYVD RLGEIKIPSL
VCSGISDLCS PLVAKTIADG IPVSKWILWE NSRHTCFVDR HDDYCRVLIE WLNEHDK
//
