ID A0A1Z3HNK2_9CYAN Unreviewed; 316 AA.
AC A0A1Z3HNK2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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=XM38_026910 {ECO:0000313|EMBL:ASC71737.1};
OS Halomicronema hongdechloris C2206.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC Halomicronema.
OX NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC71737.1, ECO:0000313|Proteomes:UP000191901};
RN [1] {ECO:0000313|EMBL:ASC71737.1, ECO:0000313|Proteomes:UP000191901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2206 {ECO:0000313|EMBL:ASC71737.1,
RC ECO:0000313|Proteomes:UP000191901};
RX PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA Scheer H., Willows R.D., Chen M.;
RT "Characterization of red-shifted phycobilisomes isolated from the
RT chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL Biochim. Biophys. Acta 1857:107-114(2016).
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; CP021983; ASC71737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z3HNK2; -.
DR STRING; 1641165.XM38_14235; -.
DR KEGG; hhg:XM38_026910; -.
DR OrthoDB; 9775557at2; -.
DR Proteomes; UP000191901; 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:UP000191901}.
FT DOMAIN 36..296
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 294
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 316 AA; 35779 MW; 2F55C79FF83D0BC1 CRC64;
MRQLYPALDP YYQGYLPVSD LHTLYFEESG CPEGQPVVFL HGGPGGGTQA IYRQFFDPHQ
WRIVLFDQRG CGQSTPHAEL TENTTWHLVA DIERLRSHLG IDRWIVFGGS WGSTLALAYA
QSHPDRCRGL ILRGIFTLRP QEIRWFYQAG ANHLFPDAWE QYLAPIPPEE RHDLVGAYYR
RLTNPDPAIC QAAARAWSVW EASTSKLLPD ASLMEKFSQD EFAVAFARIE CHYFIHGGFF
EPPDQLLRQV DQIRAIPGVI VQGRYDVVCP MITAWELHRA WPEADFIVVP NAGHSATEAG
ILSALVDATD RFAQLS
//
