ID A0A139SIR8_9GAMM Unreviewed; 887 AA.
AC A0A139SIR8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:KXU34447.1};
GN ORFNames=AXE65_07195 {ECO:0000313|EMBL:KXU34447.1};
OS Ventosimonas gracilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ventosimonadaceae; Ventosimonas.
OX NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU34447.1, ECO:0000313|Proteomes:UP000072660};
RN [1] {ECO:0000313|EMBL:KXU34447.1, ECO:0000313|Proteomes:UP000072660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV58 {ECO:0000313|EMBL:KXU34447.1,
RC ECO:0000313|Proteomes:UP000072660};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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:KXU34447.1}.
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DR EMBL; LSZO01000214; KXU34447.1; -; Genomic_DNA.
DR RefSeq; WP_068392965.1; NZ_LSZO01000214.1.
DR AlphaFoldDB; A0A139SIR8; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000072660; 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:KXU34447.1};
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:UP000072660};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 51..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 453..557
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 562..886
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 887 AA; 100735 MW; 636611FC97FE8B2C CRC64;
MQNQKPIIVR LEDYRVADYL IDKTDLSFYL REQETWVQAK LHIRRNPEAG EGLPELALNG
EQLDLLEVKL NGQLLPPAHY QVDEQFLRVQ PQQEGFVLET KVRIYPHKNT ALEGLYQSAA
GSMYCTQCEA EGFRKITYYL DRPDVMSRFS VRITADKARY PLLLSNGNLI ESGNGENNSE
HFALWHDPFP KPCYLFALVA ANLSCAEDQF ITQSGRKVTL RIYAEPSYIE QVGHAMTSLK
KAMRWDEEVY GREYDLDLFM IVAVDDFNMG AMENKGLNIF NTSCLLAHPQ TATDAAFQRV
EAVVAHEYFH NWSGNRVTCR DWFQLSLKEG FTVFRDAAFS ADMNSPTVKR IDDVRLLRTQ
QFAEDAGPLA HPVRPSSYME ISNFYTLTVY EKGAEVVRML HSLLGAETFR QGSDLYFARH
DGQAVTCDDF VQAMQDASGQ DLTQFKRWYS QAGTPQLAVR GEYLAEEKRY LLHFTQSCPP
TAELADKQPF VIPVKLALLE QQGDELPLHL TGEREAQGTC RVIPITKAVQ SVCFENISSE
PVPSLLRGFS APVKLDFAYS REQLCFLMQH DADGFNRVEA AQQLSLQVLQ DLITQRQNGS
PWQLDPLLIK ALQRVLTDNR LEAAMVAEML SLPSEAWLVE RAEIANIEAI HHAREYARRH
LADALHPLLR ARYQQLRETS RNTPFAASAE HFARRALQNT ALGYLMQTDD DQVLAACLEQ
FAQSDNLTER LAALVALVNS THIQEREQAL ASFATQYQAY PLVMDGWLAV QASSPLYGTL
EKVRELMRHA AFNLNNPNRA RALIGSFCNQ NLLQFHQADG SGYRFLADCV LQLDRLNPQT
AARLLTPLTR FRKYDEKHQA LMQSELARLQ QAHLSKDVFE LVSKSLG
//
