ID A0A0A7EG65_9GAMM Unreviewed; 868 AA.
AC A0A0A7EG65;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:AIY65640.1};
GN ORFNames=OM33_11085 {ECO:0000313|EMBL:AIY65640.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY65640.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY65640.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY65640.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP009888; AIY65640.1; -; Genomic_DNA.
DR RefSeq; WP_038641704.1; NZ_CP009888.1.
DR AlphaFoldDB; A0A0A7EG65; -.
DR STRING; 1348114.OM33_11085; -.
DR MEROPS; M01.005; -.
DR KEGG; pseo:OM33_11085; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000030341; Chromosome 1.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
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:0000313|EMBL:AIY65640.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000030341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 93..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 229..440
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 447..547
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 552..866
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 868 AA; 98493 MW; 237DD84405FF35DC CRC64;
MSEQHISTNQ AKYRKDYKAP DFLVDSLYLE FDLQPTQTRV LQKSHYKRVT ENESDLWLDG
VNQTLHCINV NGVPFSQYEQ FEQGILLKNL PSEFELHIES EIDPQNNTSL EGLYLSDGAY
CTQCEAEGFR KITYFQDRPD VLTKYTVKVI ADKSFTHLLS NGNKIESGEL ADGRHFNVWQ
DPYNKPSYLF ALVAGDFDVL QDTFKTRTGR DVLLELFVDK GNLNKADHAM ASLKRAMKWD
EERFDLEYDL DIYMIVAVDF FNMGAMENKG LNIFNSKCVL ANQATATDRD YHTIESIVGH
EYFHNWTGNR VTCQDWFQLS LKEGLTVFRD QEFSSDIGSR ALNRIDAVKV MRGPQFSEDA
GPMAHPIRPD KVIEMNNFYT VTVYDKGSEV IRMMHTLLGE TNFQKGMKLY FERHDGTAAT
CDDFVSAMQD ASNIDLTLFS KWYSQSGTPE LNVDRHYNES DKTLTLTVTQ YTAPTQDQSE
KQALHIPLAI EVISPKGISQ PLQINGEVVG NVVSLKSETH QYIFENIEQD SAVVFLEDFS
APCKVEFDQS LDELITIVKH ARSDFSKWDA MQRLMIVCLK SSIDSGSELP KMVLDLFNEL
LSSESKDLAL LSELITLPSF DAIAATYKTV PVDKICAQLA GYKSTLAMEL KDSLVQLYTS
LDENGGLDAH SISVRALKGC ILSYLALTDW DQASHELEQQ FTDSNMTNSL NALSAVCDSL
HSVHSEFLTR FKEKWQHDVL VLDKWLAQVG RLKSENITAT ITEMFANGEV DITNPNRVRA
LLMSYCMFNP QAFHAVDGSG YTLLTDLLIK LDKINPQNAA RLITPLMSYK RHTIERQNKV
KEQLKRLADI SDLSPDLYEK VSNALNGE
//
