ID A0A369UQZ1_9GAMM Unreviewed; 587 AA.
AC A0A369UQZ1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DVJ77_04225 {ECO:0000313|EMBL:RDD82733.1};
OS Dyella tabacisoli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=2282381 {ECO:0000313|EMBL:RDD82733.1, ECO:0000313|Proteomes:UP000253782};
RN [1] {ECO:0000313|EMBL:RDD82733.1, ECO:0000313|Proteomes:UP000253782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L4-6 {ECO:0000313|EMBL:RDD82733.1,
RC ECO:0000313|Proteomes:UP000253782};
RA Zhou X.-K., Li W.-J., Duan Y.-Q.;
RT "Dyella tabacisoli L4-6T, whole genome shotgun sequence.";
RL Submitted (JUL-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}.
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:RDD82733.1}.
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DR EMBL; QQAH01000003; RDD82733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369UQZ1; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000253782; 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; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 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:UP000253782};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..587
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016902118"
FT DOMAIN 61..235
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 337..489
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 587 AA; 66165 MW; B012155046B39284 CRC64;
MTLRPRLLTL ALATLLGTSA TWAADKPATQ AAAPAQPPLS EQTIRSGGVM PAEQARVHFD
HAELRIAIDP TQERIDATAT LSFTARAATD VLLLDLDHNL PISGIRLNGK PLPVTAWSNP
DGRLRIQLPA MLAVGGKVQV EVRYGGKPHT AHRAPWDGGF VWSKTPDGQP WVASAVEGEG
CDLFWPCIDQ PQGKPDLVDL YVTVPKPLAA PGNGVLIDIK DEGDKRTYHW RAKHPTTYAI
SINVGPFELL QANYSSRYGN TIPMQFWYLH GNEQQAKALF EEFPRMLDFF EQEIGPYPFG
DEKMGVVETP HLGMEHQTIN AYGNGYAKGP YGFDWLLQHE FSHEWFGNQV TNADWDDMWI
HEGFGTYMQP LYGQYLYGDM PYFSMLHDER TKLKNAYPVV AGRSQFEHEV YDAEHGPGND
IYYKGSLMLH TLRELIGDKA FFESTRRLVY GRPDPKPGNF TPRYANTRDY IDIVNQVTGR
DLHWFFDVYL YEAALPKLDM QRQGDTLTLR WQVPHDKPFP LPVEVQVGDT VRTLPMEHGE
GRIDVPAGTL VIVDPRSKLL RELPHVPEYL RWLQQKAAKS AKPAAAK
//
