ID A0A2R8AX26_9RHOB Unreviewed; 849 AA.
AC A0A2R8AX26;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:SPF80596.1};
GN ORFNames=PRI8871_02406 {ECO:0000313|EMBL:SPF80596.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF80596.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-2018) 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; OMOJ01000004; SPF80596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AX26; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000244904; 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:SPF80596.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SPF80596.1};
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:UP000244904};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 104..179
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 219..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..848
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 849 AA; 94646 MW; 562B86DB07B8B853 CRC64;
MKDAAPQTFY LSDYTPFGYE VRDVALRFVL SPSATRVHSR ITFAPNPAAS DKTFFLHGEQ
LKLIRAAING AEVTPNITPE GLTCDVPDSE FVWEAEVEIA PAENTALEGL YMSNGMYCTQ
CEAEGFRKIT YYPDRPDVMS TFTVRIESDL PIMLSNGNPG ETGAGYAEWH DPWPKPAYLF
ALVAGDLVGH ADTFTTKSGN QVDLNIWVRP GDEDKCAFGM QALKDSMKWD EDVYGREYDL
NTFNIVAVDD FNMGAMENKG LNIFNSSCVL ASPATSTDAN FERIEAIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVFRD AQFTSDMRGE AVKRIHDVIE LRARQFPEDQ GPLSHPVRPE
QFQEINNFYT ATVYEKGAEV IGMLKRLVGD DAYAKALDLY FDRHDGQACT IEDWLTVFED
ATGRDLAQFK RWYSQSGTPR LSVTDSYQDG TYTLTFKQST PPTPGQMVKD PKVIPIAVGL
LGPNGDEVQP TVTLEMTDAE QSFAFDGLGS KPIPSILRGF SAPVVLDRDT SAEERAFLLA
HDTDPFNRWE ANRELARTTL IAMIRDDAAP DEAWLEGLER VITDTTLDAN YRALMMSGPS
QSELAQTLHE MGITPDPDAI WTASDRLGQT MAERWEAHLP GLLAESTVTE AYRPDSHQAG
QRALGAAVLA LQTRLDRGAS ARAQFETADN MTLQLSALTC LVRSGNDEEA LSSFAAQWKD
DRLVMDKWFG MQIAATLPDR AADRAKALTE HPAFDWKNPN RFRAVFGSLS MNHAGFHRAD
GASYDLLADW LITLDDKNPQ TTARMCSAFQ TWKRYDAGRK AKMQAALERI QGKDGLSRDT
AEMVGRILS
//
