ID G0HJQ8_THES4 Unreviewed; 422 AA.
AC G0HJQ8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Diaminopimelate aminotransferase {ECO:0000313|EMBL:AEK73151.1};
GN OrderedLocusNames=GQS_06265 {ECO:0000313|EMBL:AEK73151.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73151.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73151.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CP002920; AEK73151.1; -; Genomic_DNA.
DR RefSeq; WP_014012833.1; NC_015865.1.
DR AlphaFoldDB; G0HJQ8; -.
DR STRING; 1042877.GQS_06265; -.
DR GeneID; 11015927; -.
DR KEGG; the:GQS_06265; -.
DR PATRIC; fig|1042877.9.peg.1227; -.
DR eggNOG; arCOG01107; Archaea.
DR HOGENOM; CLU_021802_2_2_2; -.
DR OrthoDB; 24854at2157; -.
DR Proteomes; UP000000874; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01910; DapE-ArgE; 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 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AEK73151.1};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:AEK73151.1}.
FT DOMAIN 206..318
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 422 AA; 47694 MW; 217C57F8AC428397 CRC64;
MSEALEKVSQ EIEKLQDEMV KALVELIKIP AISPDYGYEG EYDKAQKLLE MIKDWPFDKV
EVYNAPDERA KNGVRPSILA YYYGQDGEKS PRIWILTHID VVPPGDMSKW TVTEPFKPVV
KDGKIYGRGS EDNGQSLVAS LYAVKAMMNL GIRPKRTVIL AFVSDEETGS KYGVEWLMRE
HPELFRKDDL VLVPDGGNED GTFIEVAEKS ILWLRVKVRG KQVHASMPDK GLNAHRVALD
FAYHLDRFLH EKYGERDELF DPPESTFEPT MVHGPADSPN IAPGEHEVVF DCRILPRYSI
DDILADAKAL AEEVKEKYRK EFDGKVLPEI ELEILQRMDA PEPTDPNSEI VRLLQEALRR
LRGKEAKVGG IGGGTFAAYF RKLGIPAVVW ATLDEMAHQP NEYAWIKNLV EDAKVMAALA
LL
//
