ID E7RXP7_9BURK Unreviewed; 917 AA.
AC E7RXP7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
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:EFV94721.1};
GN ORFNames=HMPREF0551_1468 {ECO:0000313|EMBL:EFV94721.1};
OS Lautropia mirabilis ATCC 51599.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Lautropia.
OX NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV94721.1, ECO:0000313|Proteomes:UP000011021};
RN [1] {ECO:0000313|EMBL:EFV94721.1, ECO:0000313|Proteomes:UP000011021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV94721.1,
RC ECO:0000313|Proteomes:UP000011021};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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:EFV94721.1}.
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DR EMBL; AEQP01000010; EFV94721.1; -; Genomic_DNA.
DR RefSeq; WP_005673749.1; NZ_GL636062.1.
DR AlphaFoldDB; E7RXP7; -.
DR STRING; 887898.HMPREF0551_1468; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_4; -.
DR Proteomes; UP000011021; 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; 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 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:EFV94721.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EFV94721.1};
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:UP000011021};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 260..484
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 490..590
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 594..914
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 917 AA; 102927 MW; 71923CD5DAC1C880 CRC64;
MTFPAASQSA QPASVLPQPT VVRREDYREP DWLADGLVLH FALDAQDTVV TAACRYRRRP
GAAADAPLRL DGEALETLGV AIDDQVLPQE AWVQDKGQLV LSNLPEHFTL HTQVRIHPSA
NLELSGLYAT GSTLLTQCEA QGFRRITWFQ DRPDVMTTYR VILQARRAQY PVLLSNGNLL
AADAPAAAEA RAALSVLPLP ATDGDWHEAV WEDPFPKPCY LFALVAGNLA VNETRHRLAS
GREVLLQVWT EPEQIHRTDF ALRSLEKAIA WDERRFGLEL DLDRFMIVAA PDFNMGAMEN
KGLNIFNAKY VFADPFVATD TDFEWIESII GHEYFHNWTG NRVTCRDWFQ LTLKEGLTVF
RDQEFTADQM AAGVDAQAAG SVRAVQRMGN VRVLRQVQFA EDAGPMRHPI RPDSYQAIDN
FYTATVYEKG AEVIRMLQTL LGVDGFRRGM DLYFERHDGQ AVTCEAFVAA MADANGRDLE
QFLRWYATAG TPRLQVRSQY DAANKRLVLS LTQLLPDAEG HAMPAGERAL HIPVDVALLA
RDSGQVQQHR LLELTASQQD FVFEGVESAD ARGPMLSLLR DFSAPVVVDH PYSDEDLAFL
LRHDDNLFNR WEAGQQLAER ALLQAIRQGD AQATLKALSG ALAATLPDAR LDDGLRQQFL
MLPEEKRLAE QLEPLDPSLL RARRLAALRT LVQPLVPYLQ DVVARQHWRA NYSLAVPEVG
QRALANTALQ LLTLVGAEGA ARQARAQFEG ANNLTDRLGA LQALVQCEPD DADWALARFE
DIYRNETHVL DKWFAVQARM HGTHQPTLAR VRQLMQHPGW NSQNPNKVRA LLYTFFADNL
AEFHRPDGEG YTLWRDEVLR LDRSNPQLAA RMARTLDRHQ RFVPVLARQM HAVLEHVAHE
AQSPDVREVI AKELGAL
//
