ID A0A162DMM7_9FLAO Unreviewed; 694 AA.
AC A0A162DMM7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=AWE51_04405 {ECO:0000313|EMBL:KZS42698.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS42698.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS42698.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS42698.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-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:KZS42698.1}.
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DR EMBL; LQRT01000002; KZS42698.1; -; Genomic_DNA.
DR RefSeq; WP_066310886.1; NZ_LQRT01000002.1.
DR AlphaFoldDB; A0A162DMM7; -.
DR STRING; 1642818.AWE51_04405; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000076715; 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; cd09603; M1_APN_like; 1.
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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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:KZS42698.1};
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:UP000076715};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..432
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 694 AA; 80332 MW; 63EC949CD09BEAAA CRC64;
MRIILYLIIL LIPGVGITKQ IDAVDFLTGN VNISVHPDTK EVSGKVIYTF TMLQSTTSVY
IDAQKMNIKT VMLDGNEINI NYDDKKIVIA SDFKEKTNHT VEIEYTATPK KALYFVKDYQ
NNDQIWTQGQ GKYTSNWLPS FDDMNEKVEF DLTINYHKGY EVIANGKLIK NDAVNDSIQS
WQYDMKQPMS SYLLALAIGK YDKVVETSAE GIPLEMYFYP EDKDKFETTY RHSKRIFDFL
EKEIGYAFPW QNYKQIPVKD FLYAGMENTG ATIFSDAFVV DETAFVDRNY INVNAHELAH
QWFGDLVTET EGTHHWLQEG FATYYALLAE KEIFGEDYFL YKLYESAEQL TQLSKTPKAT
SLLDPKASSL TFYQRGAWAI YALRKKIGET SFKITIHNFL EKYKFKNATT DNFIAVAEEV
SNTDLGEFKK LWLESVTFPS QEALDLLTTS TFIKKYLGLA QERTQPLAGK WGTLAKALDF
PVNDYIGQEV IYQLGGKTSP EIIALYDKAF ETNNIFVRQA IANVLSNIPS ELRTQYESLL
KDKSYATIEP ALYHLWSSFP KNRKQYLEDT KNITGFNDKN IRILWLVLAL STKDYEIENH
QKFYFELSGY TSAKYHFSTR ENAFTYLESL QAFSDESLKN LVDGATHHNW RFRNTCRKIL
DKLLKDEKYK KKYVVLKNNL PKNQQDFLSK KLTP
//
