ID E0SRJ2_IGNAA Unreviewed; 414 AA.
AC E0SRJ2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN OrderedLocusNames=Igag_0429 {ECO:0000313|EMBL:ADM27267.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27267.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM27267.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
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 -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CP002098; ADM27267.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SRJ2; -.
DR STRING; 583356.Igag_0429; -.
DR KEGG; iag:Igag_0429; -.
DR HOGENOM; CLU_021802_2_3_2; -.
DR BioCyc; IAGG583356:GHAH-432-MONOMER; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000001304; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR001261; ArgE/DapE_CS.
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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 194..306
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 414 AA; 46182 MW; E330F8D04AB02496 CRC64;
MSREIDIRID KEMKWALDVL INMINIPTVN PPGKSFYDFA EYISKVMESI GMSVKVIEVP
RDIVEKICRE CADSPRYIVI GRIDGGKPVI QFNGHYDVVP AGEGWSFDPF KAFIDGDKVY
GRGSVDMKGG IASILLAVKI FTSIYREFNG SIEIALVPDE EIGGDSGTGY LVSEISRPNY
AIIAEGSGSS NIWIGHKGAL WGYIEVYGTQ SHGSTPWRGI NAFEYMSKIV MRIIDEYKPF
IEMRKSSYDY GDPKGNIPTI NIGGEVRGST KINIVPGYYA FSFDRRIIPE ENIDDVEMEL
KSFVDRLRRI YPEVNIEMKV VNRLAPAITK PDSILVKIAI ESIENALGIK PKPIVCLGGL
DLHYYTEKGI DAISYGPGPE ENAHIANEYV LISEIRNVAK SYVYMLSKLL GVDT
//
