ID G0L464_ZOBGA Unreviewed; 686 AA.
AC G0L464;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=zobellia_4552 {ECO:0000313|EMBL:CAZ98687.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ98687.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ98687.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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; FP476056; CAZ98687.1; -; Genomic_DNA.
DR RefSeq; WP_013995874.1; NC_015844.1.
DR AlphaFoldDB; G0L464; -.
DR STRING; 63186.ZOBELLIA_4552; -.
DR KEGG; zga:ZOBELLIA_4552; -.
DR PATRIC; fig|63186.3.peg.4465; -.
DR HOGENOM; CLU_394736_0_0_10; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000008898; 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; 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; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 1.
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:CAZ98687.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAZ98687.1};
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:UP000008898};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..196
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 686 AA; 79451 MW; F38AAFDFD44F46DF CRC64;
MRYFLLLLFF GFVSFSFGQH QDKVDFVRAD VYIEPVPLNK EIIGRVVYRF KVLQNVDSVF
LDAKDMRFEK VEMNGKQVDF IATDKTISIR KKLKKDTSHE LTIAYVAKPR QTVYFLGWGD
KIEGNEQVWT QGQGKYTSHW LPSFDDMNEK VEFDLAIQAN QTYEVIANGK LLSVSKGENG
RPVWLFDMEN PMSSYLLAFA IGHYSKQELS SSTGVPILNY FYPQDSARVE PTYRHTRRIF
DFLEDEIGVS YPWQDYKQIP VRDFLYAGME NTGATIFSDG YVIDATAFVD KNYVNVNAHE
LAHQWFGNLV TEKDGSHHWL QEGFATYYAY LAEKKIFGDD HFYWKLFDTA KELREISEGG
KGQALVDPKA SSATFYEKGA WALVMLRELV GDKPFKKGVS DYLNTHRFKN VTIDDFLREM
ERASAVNLEG FRVKWLESSE FPWDEAKTYL MDKNEALSAF LGSGHELKDL EKELQAERPV
QYKEALVDEL AQEILDKDRF APLFDHPQLK VRQKAIQLID QISSIHKESA EKLLDDTSYI
TQELALFKLW SSFPESRKAY LDATKEVIGL PNKNVRLLWL FLAVATEGYE AENTRKYFAE
LTAYTSPEQG WEVRIGAFQY LREIGFTDEG LANLINATNH HSWQFKKYAR GLIGQLLEDQ
EYKTRIEKLV GKLNQEETRY ISTKLN
//
