ID K8GM60_9CYAN Unreviewed; 859 AA.
AC K8GM60;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=OsccyDRAFT_2341 {ECO:0000313|EMBL:EKQ69700.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ69700.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ69700.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ69700.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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:EKQ69700.1}.
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DR EMBL; AJUB01000010; EKQ69700.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GM60; -.
DR STRING; 864702.OsccyDRAFT_2341; -.
DR PATRIC; fig|864702.5.peg.2518; -.
DR eggNOG; COG0308; Bacteria.
DR eggNOG; COG1413; Bacteria.
DR HOGENOM; CLU_014298_0_1_3; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000001332; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
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; cd14686; bZIP; 1.
DR CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
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; PF13646; HEAT_2; 2.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM00567; EZ_HEAT; 6.
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:EKQ69700.1};
KW Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001332};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..208
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 244..453
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT COILED 823..857
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 859 AA; 97300 MW; 6F44D9F9A84A1062 CRC64;
MPQHLFGFDN KNGHRSFELP GARPHYSPDR PGQVEHIFLD LDLDIPKQRY SGTCHIHLNP
VRTGIDRLTL DAVNLTIESV AVDEIPQHFE YDGEQLQIQL QPPTTAGKTV TLAIAYHVAQ
PQRGLYFIAP NQHYPHKPVQ VWTQGEDEDS RFWFPCFDYP GQLATSEIRV RVPKNLIAIS
NGELISTEED GNSKIFHWSQ KEVHPTYLMT LAVGDFAELR DEWNGKPVIY YVEKGKEAAA
RLSMGKTPQM IEFFSQKYGY PYAFPKYAQV CVDDFIFGGM ENTSTTLLTD RCLIDERAAI
DNRSTESLVA HELAHQWFGD LVVIKHWSHA WIKEGMASYS EVMWMEHEYG AEEAAYYRLG
EARSYLDEDA SRYRRPIVTH VYREVIELYD RHLYEKGACV YHMIRAELGD DLFWQAIATF
VNDNAHRTVE TVDLLRAIEK ASGRNLLFLF DQFVFRGGHP DYSVAYSWDG DSNLAKLTVT
QTQAKDNSDR ANLFDLKIPI GFGYIGEPES KPLNVRVRER EQSFYFPLEK KPDYVRFDVG
NHTLKTVILD YPIPELKAQL QNDPDPLARI YAAEALAKKG GLESVKILSE ALAQDSFWGV
RAEIARNLAS IKLDQTFSGL LIGLKDIDAR VRRATVESLA GIKTTESYKA IKPLAEKGDA
SYYTEAAALR ALGSLAGSNL LNEKEEKTLK LLKSVLKERQ GWNEVVRAGA IAALSQMKTS
EAALDLILEY TELGVCQPLR LAAIRALGTI STGQTNVNLE RILNRLQELS RESFFLTQVS
VVNALGQMET PKAIPILDSL AHHTSDGRVR RIAEEAMQKV QKNVGSDQAM KQLREELDQI
KQENQELKSR LEALEARVK
//
