ID A4AQB0_MARSH Unreviewed; 529 AA.
AC A4AQB0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Aminopeptidase M1 family protein {ECO:0000313|EMBL:EAR01649.1};
GN OrderedLocusNames=FB2170_14013 {ECO:0000313|EMBL:EAR01649.1};
OS Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR01649.1, ECO:0000313|Proteomes:UP000001602};
RN [1] {ECO:0000313|EMBL:EAR01649.1, ECO:0000313|Proteomes:UP000001602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX PubMed=21037013; DOI=10.1128/JB.01207-10;
RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT Maribacter in the family Flavobacteriaceae.";
RL J. Bacteriol. 193:303-304(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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DR EMBL; CP002157; EAR01649.1; -; Genomic_DNA.
DR AlphaFoldDB; A4AQB0; -.
DR STRING; 313603.FB2170_14013; -.
DR KEGG; fbc:FB2170_14013; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_014298_1_1_10; -.
DR Proteomes; UP000001602; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR034015; M1_LTA4H.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:EAR01649.1};
KW Hydrolase {ECO:0000313|EMBL:EAR01649.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Protease {ECO:0000313|EMBL:EAR01649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 33..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 276..453
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 393
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 529 AA; 61665 MW; 0B978CC2CE92EE66 CRC64;
MFLVVLGLPA QEFTEQDTLR GSITPERAWW DLNYYHLDIE VKPDEKYISG TNLIRYKVLE
EEKVLQIDLQ PPLQIEKVTQ DGKKLKVESN GNAHFIKLRK KQKKGDFNEI IVHYSGHPKE
AERAPWDGGF SWKKDENGKH FVATSCQGLG ASVWWPNKDH MYDEVDSMAM SVKVPKGLMN
VSNGRLLKVE EDTNTYHWFV ANPINNYGVN VNVGEYVHFG EKYKGEKGIL DMDYYVLRDN
LEKAKEQFKQ APMTMRAFEH WFGPYPFYED SFKLVEVPYL GMEHQSSVTY GNHYQNGYLG
RDLSGSGWGL LFDFLIIHES GHEWFANNIT DIDIADMWVH EGFTSYSENL YLDYHFGTKA
AEEYVIGLRK NIQNDRPVIG HYNVNNSGSG DMYYKGSNLL HNIRQLVDND EKWRQILRGL
NKDFYHQTVS SAQIEQYLID KTGIDLSTIF DQYLRTIMIP TLEYKIDGKN LEYRYTNVVD
EFKMPIRLFI DGEVQWIDPT QDWQTTSIEG DLSTLQIDKN FYIEIKPDN
//
