ID A0A171KPC4_9BURK Unreviewed; 902 AA.
AC A0A171KPC4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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 ORFNames=AAV32_14655 {ECO:0000313|EMBL:KKO70741.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO70741.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO70741.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO70741.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-2015) 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:KKO70741.1}.
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DR EMBL; LBNE01000012; KKO70741.1; -; Genomic_DNA.
DR RefSeq; WP_068373896.1; NZ_LBNE01000012.1.
DR AlphaFoldDB; A0A171KPC4; -.
DR STRING; 206506.AAV32_14655; -.
DR PATRIC; fig|206506.3.peg.3123; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000078084; 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:KKO70741.1};
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:UP000078084};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..456
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 467..575
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 578..901
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 902 AA; 99669 MW; 63106707BCC1D906 CRC64;
MRHASPTTIL RQDYQAYPFQ IPSIELEFDL AAETTRVISR LHVQRKPDAP AQAALVLDGE
ALTLQSIHVD GQLLDASRYQ VDDASGTLRI DGLPADAQVQ ITSLCRPAQN TTLMGLYVSG
ASLFTQCEAE GFRRITWFAD RPDVMSRYRV TLRASQADYP LLLSNGNLIE TTTLDGGRHQ
AVWEDPHPKP CYLFALVAGQ FDCRESRLRT RSGREALLQV YADPGSGTQT AWALESLERS
VRWDEQRFGL ELDLDRFMIV AARDFNMGAM ENKGLNVFNA AYVLADPQTA TDANYRAIEA
VIGHEYFHNW TGNRVTCRDW FQLSLKEGLT VFRDQEFTAD MMAAGLDAEA AASARTIKRI
DDVTVLRAAQ FPEDAGPMAH PIRPDSYQEI GNFYTATVYE KGAEVIRMQH TLLGEAGFQE
GIREYFRRHD GQAVTCDDFV NAMESVYKRL HSGKDLAVFR RWYEQAGTPR VRVELDYDAA
TRSCVVTLSQ SNPPVGVEKE RGADFIKAPL HIPFAIGFIA ADGQALTPVL NGQQADTFLL
ELTEARQQWR FENMASAPTP SLLRNFSAPV IVDYDWQDAD LALLSAHDGN PFARWEAGQE
LAARQVLANA ARLRGGEPMH ADPVFVDAWR AQLSAPGLDA GYRARALALP SEKALAQRME
KMDPPAIAAA RDFLRAELGR TLTPLWRAAY DANEVAGPYS PDAPSAGKRA LRNLALAYLL
AGQAEGAREL ALAQYDAASN MTDGLAALTA LVNDSRDAAT EQRLAAFYET WKHDPLVVDK
WFALQASSRA TDVAAARRLL THPAFTLRNP NRARSLVFQF CLNNPAGLHQ ADGAGYAFWT
EQVLALDAIN PEIAARLARA LDNWAAHAPA LSAPMRAAIE RVRAHQPLSR NVDEITAKAL
AL
//
