ID H0Q252_9RHOO Unreviewed; 896 AA.
AC H0Q252;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:BAL25751.1};
GN ORFNames=AZKH_3462 {ECO:0000313|EMBL:BAL25751.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL25751.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL25751.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL25751.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) 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; AP012304; BAL25751.1; -; Genomic_DNA.
DR RefSeq; WP_015437053.1; NC_020516.1.
DR AlphaFoldDB; H0Q252; -.
DR STRING; 748247.AZKH_3462; -.
DR MEROPS; M01.005; -.
DR KEGG; aza:AZKH_3462; -.
DR PATRIC; fig|748247.4.peg.3417; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_4; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000007106; Chromosome.
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:BAL25751.1};
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:UP000007106};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 120..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..454
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 459..563
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 567..895
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 896 AA; 98692 MW; 0BAD24C9385DA19B CRC64;
MKTDQAPSIE RSDYRPLPWR VDHVELHFAL DEEATVVTSR LRCTRNRQVS AGPLRLLGEE
LELLGLTVDG AAPVDGQLAR GEGWLELTLA GDTAEIGVVT RIDPRANTTL SGLYVSRGGF
FTQCEAEGFR RITYFPDRPD AMARFTVTLE GDAERHPVLL SNGNLIEQGK LDGGRHYAKW
EDPFPKPSYL FALVAAKLVA LERRVTTASG REVLLQVWVE DGNLDRTGHA MESLVHSMRW
DEEVFGLELD LDRFMIVAVS DFNMGAMENK GLNIFNAKYV LAKPETANDV DYENIESVVA
HEYFHNWTGN RVTCRDWFQL TLKEGLTVFR DQEFSADMLA QAAGAEGAAS ARAVKRIDDV
RVLRAAQFPE DAGPMAHPIR PESYHEINNF YTATVYEKGA EVIRMLHTLL GAEGFRNGMD
LYFSYHDGQA VTCDDFVDCM AEANGVDLDQ FMRWYSQAGT PRLRATGSYD AAGHRYTLTL
SQHTLPTPGQ AEKLPLAIPV AVGLIGPDGK DLPLRLEGEL HAGGTTRVLE LKGAEQSFVF
ADVSAEPVPS VLRGFSAPVI LEVDEDDARL AFRMAHDTDA FNRWDAAQRF AERVILGLTA
DVAAGKALHV PESFVAAFRA MLTDGTLDPA FRAQAAALPS EGYLLERMAV ADPGPLRTAL
IHLTRAIGAR LANDWLSLYK TLEVSGPYRY HPGDAGRRAL CNLALKYLVA AGSVEGFDLA
RAQFARFGNM TEGSGALAAL MNDGGVERDA ALADFHSRFR DDALVLDKWF ALQAGAWRWD
AVTPPVLERV KALMDDPAFS LTNPNKVYAL LGSFFRANPA EFHAVDGSGY AFWADQVIAL
DRCNPQVAAR TARALENWKR YAPALQTLIR SQLERVRAIE GLSPDVAEIV AKALAD
//
