ID A0A3B0C9M6_9FLAO Unreviewed; 692 AA.
AC A0A3B0C9M6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=D7Z94_10140 {ECO:0000313|EMBL:RKN81288.1};
OS Ulvibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacterium.
OX NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN81288.1, ECO:0000313|Proteomes:UP000276603};
RN [1] {ECO:0000313|EMBL:RKN81288.1, ECO:0000313|Proteomes:UP000276603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM003 {ECO:0000313|EMBL:RKN81288.1,
RC ECO:0000313|Proteomes:UP000276603};
RA Zhang Z.;
RT "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT prolifera.";
RL Submitted (OCT-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:RKN81288.1}.
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DR EMBL; RBCJ01000002; RKN81288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0C9M6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000276603; 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:UP000276603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..434
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 692 AA; 80668 MW; 477FE53297B7353D CRC64;
MKQLITVLFL FQSVFVLTQR QDKVNFIHGE AQIVPFAREG RLEGSVIYKF EVFQDVDSVF
LDARNMEFTS VRLNDRIVKY SNSGNTVSLK KKLKGGKSYK LKLDYTAGPK QTVYFMNWND
DNPNNDQIWT QGQGKYTSYW LPSFDDMTEK VEFDLNITFD KNYEIIANGK LVAIQEKNSL
KTWSFDMKDP MSSYLLAFAI GIYEKQQLTS ANGTPIKNYF YPKDSERVEP TYRYTKEIFD
FLEEEIGVAY PWQNYKQVPV HDFLYAGMEN TGCTIFSDAY VIDSVAFMDK NYVNVNAHEL
AHQWFGNLVT EKSGSHHWLH EGFATYYAYL TEKELFGEEH FYWKLFETLT ALQNSIEKGQ
GQSLLDPRAS SLTFYEKGAW AIFMLRDRIG DVAFKKGIQS YLEKYAFANV TVPSFIQEME
KSSGADLSHY VKVWLEDTAL PFKVAQEKLA EKSEPLKSLF ALQAALKSQE SDDIDYTSYW
NGTNSIQLKK YMIQNFLRTM PEEIIDRVLD SNTLELRQAL ALSIQDAKDY PKEKFETLLN
DNSYVTLENT LFKLWMAYPE ERNSYLEKTK ETIGFPNKNV RLMWLTLAIL TEGYEGRNTK
LYFDELSGYT APEYSFEVRQ GAFQYLNEAF GFKDSNLLDL AEATTHHSWQ FKKFSRNLMV
ELLKDQVYKE RIMSLLGKLK PEERRYIESK VK
//