ID A0A1S1MYY3_9GAMM Unreviewed; 864 AA.
AC A0A1S1MYY3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BET10_11230 {ECO:0000313|EMBL:OHU91384.1};
OS Pseudoalteromonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU91384.1, ECO:0000313|Proteomes:UP000179786};
RN [1] {ECO:0000313|EMBL:OHU91384.1, ECO:0000313|Proteomes:UP000179786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW1 {ECO:0000313|EMBL:OHU91384.1,
RC ECO:0000313|Proteomes:UP000179786};
RA Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT seawater.";
RL Submitted (SEP-2016) 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:OHU91384.1}.
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DR EMBL; MKJU01000025; OHU91384.1; -; Genomic_DNA.
DR RefSeq; WP_070985261.1; NZ_MKJU01000025.1.
DR AlphaFoldDB; A0A1S1MYY3; -.
DR STRING; 1859457.BET10_11230; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000179786; Unassembled WGS sequence.
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:OHU91384.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..184
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 224..434
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 442..541
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 546..863
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 864 AA; 97608 MW; 4A00310284355354 CRC64;
MQTKPQAKYL KDYKAPSHQV EQLELTFDLH PTQTMVTAKA KYLALEAHNS LTLDGVDLKL
VSLKVDGKAF DDYQSTSTTL TLSSLPNEFE LEIVTEISPQ TNTALEGLYL SGGAYCTQCE
AEGFRKITYF LDRPDVLTVY TVTVIGDRAM PSLLSNGNKV AQGTLEGGRH YTTWHDPFKK
PSYLFALVAG DFDELKDEFI TRSGRKVELV LFVDKGNLSK APHAMASLKN AMKWDEERFN
LEYDLDIYMI VAVDFFNMGA MENKGLNVFN SACVLANQQT ATDRDYHTIE SIVGHEYFHN
WTGNRVTCRD WFQLSLKEGL TVFRDQEFSS DLGSRGLNRI DAVMAMRMHQ FAEDAGPMAH
PIRPNKVIEM NNFYTVTVYN KGAEVIRMMH TLLGEQNFQK GMQLYFERHD GQAVTCDDFV
AAMQDASKID LTQFKLWYEQ VGTPSLKVVT SFDAELSQYV CTITQQNAKH DPIQSPLHIP
FAIELLDKEG QALPLIVNGE RISKVINLTE EEQTITFEQI NECPVAVLLE DFSAPVIVNY
DYQLGELIHI IAHASSDYAR WEAAQQAFTL QMREAVSQFE QGQPIRLSYA LIETFDKLLR
ERKGDLALLA ELIRVPSFDT LATAFEQVPV EALNESIAEF ELAIASGLRS TLKDTFTACV
ENGELDHEAV SARALKNTCL YYLAKCADEQ VHEWLESQRT SDNMTLVLGA LKASLSAQLA
SSSAAMNEFD SHWRHDLLVM DKWFALQATQ KGDDAIKHIY DLYSHPCFDK GNPNRVRALV
GSFARNNPEQ FHRVDGKGYE LLGDLLVELN AINPQNASRM ITPFMSWKRF DAKRQQLMKS
QLQRLAAMSD LSDDLYEKVE KALS
//
