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Database: UniProt
Entry: A4IRX6_GEOTN
LinkDB: A4IRX6_GEOTN
Original site: A4IRX6_GEOTN 
ID   A4IRX6_GEOTN            Unreviewed;       470 AA.
AC   A4IRX6;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Xaa-His dipeptidase {ECO:0000313|EMBL:ABO68080.1};
GN   OrderedLocusNames=GTNG_2735 {ECO:0000313|EMBL:ABO68080.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO68080.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO68080.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO68080.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP000557; ABO68080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4IRX6; -.
DR   KEGG; gtn:GTNG_2735; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0016805; F:dipeptidase 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   CDD; cd03888; M20_PepV; 1.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          263..337
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   470 AA;  51676 MW;  A35593F074DA5641 CRC64;
     MTLNINWIEE ARKRKDDLVR DVQALVRIPS VRDDSEAQPG APFGLKVAEA LDYMLTRGQA
     EGFRVKNVDG FAGHVEMGQG EKLIGVLGHI DVVPPGDGWT VDPFSAHVRD GRIYGRGAID
     DKGPTIAAFY AMKIVKELGL PLSKRVRLII GGDEESDWRC VDHYFKHEEM PDIGFVPDAD
     FPIIYAEKGI IDADLQYRLT GSEETGEMTL RSFQAGRRYN MVPDAAEAVV EGAGLEEWSS
     RYERFCRDHG LNGNIHHSGE AAVLTLEGVA AHGAEPERGK NAGVYLAQFL ASLPLDGGSR
     PFVQFVASSF FGDTRGRKLG LAYRDERSGE LTVNVGVLSY DRAQGGTIGL NIRYPVTADG
     ETIRQTLSNV AVERGLTLGR FHDTKPHYVD PDHEWIRTLQ RIYEEQTGEP GRLLAIGGGT
     YARSLTAGVA FGALFPGRPD VAHQKDEYVE IDDLVKATAI YAQAIYELAK
//
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