ID   A0A925HY51_9BACT        Unreviewed;       781 AA.
AC   A0A925HY51;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 11.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE   Flags: Fragment;
GN   ORFNames=IAF94_02060 {ECO:0000313|EMBL:MBC7852193.1};
OS   Pirellulaceae bacterium.
OC   Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC   Pirellulaceae.
OX   NCBI_TaxID=2699754 {ECO:0000313|EMBL:MBC7852193.1, ECO:0000313|Proteomes:UP000609570};
RN   [1] {ECO:0000313|EMBL:MBC7852193.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ES-bin-42 {ECO:0000313|EMBL:MBC7852193.1};
RA   Zeng Y.;
RT   "Metagenome-assembled genomes from the Lille Firn glacier at the Villum
RT   Research Station in northeast Greenland.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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:MBC7852193.1}.
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DR   EMBL; JACNFG010000120; MBC7852193.1; -; Genomic_DNA.
DR   Proteomes; UP000609570; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR   GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF03130; HEAT_PBS; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM00567; EZ_HEAT; 4.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..152
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          187..395
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   COILED          720..778
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:MBC7852193.1"
SQ   SEQUENCE   781 AA;  88200 MW;  02CB82EC1D9F5259 CRC64;
     ASSIELDAAE MAIGEVTLAT EETANPSQKL QKNHQGNKLT IQLGKEYPAG QKLQIAIDYV
     VTKPNQGAHF VIPDASEPSQ PKMVWTQSEP EDARYWFPCF DSPNDRLTSE IVTVAPENFI
     VLSNGSLISK RENDDKTITW HWSQVKSHSP YLMSVVAGDF EVLEQNWDGI PVLSYVPRGR
     LAEAARSFDK TPAMMAFFSE KIGYRYPWPK YAQICVDEYG WGGMEHTSAT TLNLNTLHDE
     RAHADISSIN LVAHELAHQW WGDLVTCKDW GEIWLNESFA TYFATLWTEH DEGWDEAAWA
     RHQEAESYFG EDTRYRRSIV NYRYNSPMNV FDSHAYPKGG RVLHMLRFEL GDEQFWRALR
     RYAEVNQFRT VETADLRIAI EDATGQGLNW FCDQWLYHGG HPEFTVSWEW DSAAKDVKLT
     VKQTQKVEDV TPLFRTSAEI EIALPGETLI KKIQITKPEE TYHFTVAERP TRVCFDPKDW
     LLKKLTFAKS KEELLDQLAN DKNVICRLQA IQGLDSQKGD PQVAAALMTA AAKDSFWGIR
     EEAVKVIGKL NGDEARKTLI SAAKDDKKSL VRRAAVSGLG NFADDESRAA LKEVFHKDGS
     YYAAAEALRA LLKIDRDNVR DLLTAALDRP SHHEVLLRAA CDGLADLKDS AAAEKIAAML
     KSPLTPERRI VLLGALARLK GGDAAVVKQV EEQLSNDRVD VRRAAVESLV ALAQPAAIPA
     LQARREKEQH RRTLRDIDEA IAKLRDKDKS AEDLRKEVEA LRKKNEDLET RLKKLEGKGK
     E
//