ID E5BDW0_9FUSO Unreviewed; 342 AA.
AC E5BDW0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=M42 glutamyl aminopeptidase {ECO:0000313|EMBL:EFS21236.1};
GN ORFNames=FSBG_00733 {ECO:0000313|EMBL:EFS21236.1};
OS Fusobacterium gonidiaformans 3-1-5R.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS21236.1, ECO:0000313|Proteomes:UP000002975};
RN [1] {ECO:0000313|EMBL:EFS21236.1, ECO:0000313|Proteomes:UP000002975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS21236.1,
RC ECO:0000313|Proteomes:UP000002975};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 3_1_5R.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; GG657971; EFS21236.1; -; Genomic_DNA.
DR RefSeq; WP_008801306.1; NZ_GG657971.1.
DR AlphaFoldDB; E5BDW0; -.
DR HOGENOM; CLU_053520_0_0_0; -.
DR OrthoDB; 361940at2; -.
DR BioCyc; FSP469605-HMP:GTSP-738-MONOMER; -.
DR Proteomes; UP000002975; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05657; M42_glucanase_like; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF7; AMINOPEPTIDASE YHFE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EFS21236.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002975}.
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 342 AA; 38188 MW; AE2398ECF7AAC3E2 CRC64;
MNVDINYILD LTEELLSIPS PVGYTHLGIA RIAEELDKFG IRYEYTKKGA ILAFVEGENR
EYRKMISAHI DTLGAVVRNV KANGRLELTN TGGYAWGSVE GENVLVHTLS GKVYEGTLLP
VKASVHTYGD VARELPRIEE NMEVRIDEDV KKAEDVLKLG ILQGDFVSYE TRTRRLANGY
IKSRYLDDKL CIAQVFGYLK YLADTASKPK SDLYIYFSNF EEIGHGVSLF PEDLDEFISI
DIGLAAADAH GDEKKVNIIA KDSRSPYDFV LRKKLVEAAE AADIPYTVSV NYRYGSDATT
AILQGFDFKY ACIGPSVDAS HHYERTHNDG IIATVDLMIA YL
//
