ID A0A2A5X3A8_9GAMM Unreviewed; 879 AA.
AC A0A2A5X3A8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=CNF00_00205 {ECO:0000313|EMBL:PDH43151.1};
OS Candidatus Thioglobus sp. MED-G25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1986229 {ECO:0000313|EMBL:PDH43151.1, ECO:0000313|Proteomes:UP000219647};
RN [1] {ECO:0000313|EMBL:PDH43151.1, ECO:0000313|Proteomes:UP000219647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G25 {ECO:0000313|EMBL:PDH43151.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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:PDH43151.1}.
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DR EMBL; NTKC01000001; PDH43151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5X3A8; -.
DR Proteomes; UP000219647; 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:PDH43151.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..191
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..441
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 449..552
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 557..878
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 879 AA; 99855 MW; F2A376A1F6629D4D CRC64;
MTPEKTTLDR IYLSDYQPPG FLITTTVLHF ELSANNTRVR SQLSIRRRNS NQGSLRLDGE
ALELESIRVD GKELTPNQYT IDDHSLTVHD VPSQFTLQIE NYISPAANTK LEGLYLSSGN
FCTQCEPEGF RRITYFIDRP DVLSEYTVTL NASVTDCPVL LSNGNILSTE TLPNGRHQVT
WHDPHPKPSY LFALVAGDLG FIEDRFTTAS GRDVRLRIYA VERDLGQCRH ALDALIQAMR
WDELRYGREY DLDCFNIVAV EDFNMGAMEN KSLNIFNTRY VLALPETATD QDYQAITGVI
GHEYFHNWSG NRVTCRDWFQ LSLKEGFTVF RDQEFSAELG SAGVKRIEDT KLVRGPQFLE
DSGPMAHPVR PASYSEINNF YTLTVYIKGA EVVRMLANLL GPVLFRKGCD QYFDRHDGQA
VTTEAFISAM EHTSGLDLSQ FRLWYEQAGT PKLTTRGTYD AEMARYTLTV AQQCPSTPDQ
DQKKPLHIPL ATALFDRAGQ AMKTTIGAQG DPKHEHMLSL CQQEQQFVFE GVVKEPVVSL
LRRFSAPVEL ESDLSGDELA ILMAHDDDPF NRWDAGQRLF STEVLRAFEA SVEGNSFSLN
ERFAVAFENT LRHDFDDRSF QAYALALPDH THLLQITPII EPDRLHQARK TVKLILARRF
TTEFEALYHR LEATGNDQTN CINSGQRALR NTCLSYLMAL EQPEFTRLAS HQLQAADNMT
DALAALTLLA CSPHPERTAA LAHFFDRWQD YPLVMDKWFR VQATADLPGT LGHVKALTSH
DLFQLENPNK VFSLLGAFAH ANPLHFHQVD GQGYAFISEY ILKLDHTNPQ VAARLLSAFN
LWRRYNRERQ EMMREQLEQI QAQPALSKDV SEIINRILS
//
