ID A0A1I5GM27_9RHOB Unreviewed; 850 AA.
AC A0A1I5GM27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN04487859_13313 {ECO:0000313|EMBL:SFO37007.1};
OS Roseovarius lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFO37007.1, ECO:0000313|Proteomes:UP000198599};
RN [1] {ECO:0000313|EMBL:SFO37007.1, ECO:0000313|Proteomes:UP000198599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28463 {ECO:0000313|EMBL:SFO37007.1,
RC ECO:0000313|Proteomes:UP000198599};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOVP01000033; SFO37007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5GM27; -.
DR STRING; 1005928.SAMN04487859_13313; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000198599; 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:SFO37007.1};
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 91..179
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 218..432
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 437..528
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 533..847
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 850 AA; 95024 MW; 0F438A065ECEF38F CRC64;
MKDAAPQAVY LSDYTPPAYL VDEVHLTFRL AAETTRVISK IRFRPNPEAQ NRDFFLHGEG
LSLVSAMIDG AAITPEITPE GLRAVVPDAP FTFQAEVEIN PAANTALEGL YMSNGMYCTQ
CEAEGFRKIT YYPDRPDVMS VFTVRIEGDA PVMLSNGDVV AQGDGFAEWH DPWPKPAYLF
ALVAGDLINH PDRFTTRSGR DVELNIWVRP GDEGKCAFGM EALKKSMTWD EEVYGREYDL
DIFNIVAVDD FNMGAMENKG LNIFNSSCVL STAETSTDAN FERIEAIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVYRD SEFTSDMRSA PVKRISDVID LRARQFREDN GPLAHPVRPA
SFVEINNFYT ATVYEKGAEL IGMLKRLVGD AAYRKALDLY FERHDGQACT IEDWLTVFEN
VTGRDLAQFK RWYEEAGTPR LKVSDEFKDG TYTLHFEQET PPTPGQEVKQ PRVIPIAVGL
LGANGDEVQA TRVLEMTQAA QSFSFDGLAA RPIPSILRDF SAPVILERDT DNAERAFLLA
HDTDPFNKWE AGRALARDGL IAMIREDAAP DPAYLDAVQM MARDEALDPA FRALALGLPS
EDELAQSLFE MGVTPDPQAI WQALERLRNT RAKQIEDLAR ELYTAHQVTA PYRPDAEQSG
ARALANAALA MISRVDGGAL AAQQFDSADN MTQQLAAWSC LLQAGAGDAA TKAFYDQWQQ
DRLVIDKWFS LQIVHASPEH TAEAASRLAN HADFNIRNPN RFRATFGAMV TSPAGFHHAS
GKGYRVLADW LIRLDPLNPQ TTARMCSAFE TWRRYDDTRQ TLIKAELDRI LATPGLSRDT
TEMVTRIRGV
//
