ID D1Y292_9BACT Unreviewed; 388 AA.
AC D1Y292;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative selenium metabolism hydrolase {ECO:0000313|EMBL:EFB91582.1};
GN ORFNames=HMPREF7215_1440 {ECO:0000313|EMBL:EFB91582.1};
OS Pyramidobacter piscolens W5455.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Pyramidobacter.
OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB91582.1, ECO:0000313|Proteomes:UP000006462};
RN [1] {ECO:0000313|EMBL:EFB91582.1, ECO:0000313|Proteomes:UP000006462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W5455 {ECO:0000313|EMBL:EFB91582.1,
RC ECO:0000313|Proteomes:UP000006462};
RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EFB91582.1}.
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DR EMBL; ADFP01000029; EFB91582.1; -; Genomic_DNA.
DR RefSeq; WP_009163974.1; NZ_ADFP01000029.1.
DR AlphaFoldDB; D1Y292; -.
DR STRING; 352165.HMPREF7215_1440; -.
DR eggNOG; COG0624; Bacteria.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000006462; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR017706; Peptidase_M20/DapE_YgeY.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR03526; selenium_YgeY; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000313|EMBL:EFB91582.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 177..275
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 388 AA; 42212 MW; D92D02DFA14ED15D CRC64;
MIAQKFWNET HRRDLLDFYV AAVKTRSYSD QEGELAQKLL AKMKELGYDE AYVDAAGNVC
GRVGRGGRVI HFDSHMDTVL AENADEWKHP PFAGEIEDGM LYGRGAVDMK GGLTASICAA
GAAKKLGLLE GKTVWVTGSV CEEYCDGVCL EHFYRDSGVR PDFCVICEPS DNVITLGHTG
KVQARLVTHG VSAHGSAPEK GVNAVYEMAE IIQRVEALNA ALRENGGGTI VLSHISCQTA
SLNAVPDRCE IYLDRRLRLG ETTAQVATEL AALAAGKRAS VEPGTLVHTS WNGARLVYRP
EHDPWKIGES HPLTLACNAA YEKTFGEAPA RYDFWDFGTN AVVPVAMGVP TIGFGPGEYK
LAHMTDERCA LAKVEEACCF YIHLIETL
//
