ID A0A1P8F8K2_9CHLR Unreviewed; 357 AA.
AC A0A1P8F8K2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:APV44809.1};
DE EC=3.2.1.4 {ECO:0000313|EMBL:APV44809.1};
GN ORFNames=Dform_01487 {ECO:0000313|EMBL:APV44809.1};
OS Dehalogenimonas formicexedens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV44809.1, ECO:0000313|Proteomes:UP000185934};
RN [1] {ECO:0000313|Proteomes:UP000185934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT bacterium isolated from contaminated groundwater.";
RL Submitted (NOV-2016) 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; CP018258; APV44809.1; -; Genomic_DNA.
DR RefSeq; WP_076004437.1; NZ_CP018258.1.
DR AlphaFoldDB; A0A1P8F8K2; -.
DR STRING; 1839801.Dform_01487; -.
DR KEGG; dfo:Dform_01487; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000185934; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 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:SF0; AMINOPEPTIDASE YPDE-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 Glycosidase {ECO:0000313|EMBL:APV44809.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:APV44809.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000185934}.
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 357 AA; 38542 MW; 7D23ACF88FE9B731 CRC64;
MDDIEGLLKE LTEASGVSGY EREVRLILER RFAALGEVSR DRLGSVIGVQ KGSSASPRIL
IAAHMDEIGF MVKMITREGF IKFVPLGGWP NQHLPAQRVM IQTSSGPVVG VIGTPPPHLL
RDKDRNTTPD KKEMFIDIGA TSKEEVEAAG VRVGDPIVPI TDFTVLSVKE PTYMAKAFDD
RVGCALLISV MESLAGGKHP NAVYGVGTVQ EEVGLRGATT SAEMVNPDVA IILDIGPIGD
VPGIKPDESI TKLGGGPNLL VYDTRMIPNL KLRDLVMETA RQMDIPLQLD TLEFGGYDGG
AIHLHKSGVP TVVIAIPTRH AHSHNSIIRR KDYDMTSKLV TALVRRLDEA TVAGLCD
//
