ID A0A0V8RSC3_PYROC Unreviewed; 400 AA.
AC A0A0V8RSC3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=CF15_07985 {ECO:0000313|EMBL:KSW10794.1};
OS Pyrodictium occultum.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=2309 {ECO:0000313|EMBL:KSW10794.1, ECO:0000313|Proteomes:UP000053352};
RN [1] {ECO:0000313|EMBL:KSW10794.1, ECO:0000313|Proteomes:UP000053352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL-19 {ECO:0000313|EMBL:KSW10794.1,
RC ECO:0000313|Proteomes:UP000053352};
RA Utturkar S., Huber H., Leptihn S., Brown S., Stetter K.O., Podar M.;
RT "Genome sequence of Pyrodictium occultum PL-19, a marine hyperthermophilic
RT archaeon isolated from Volcano, Italy.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KSW10794.1}.
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DR EMBL; LNTB01000002; KSW10794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V8RSC3; -.
DR STRING; 2309.CF15_07985; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000053352; Unassembled WGS sequence.
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:UP000053352};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 181..294
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 400 AA; 44300 MW; E379EB00FBD18586 CRC64;
MVYLLQRLIA VPTVNPPGEH YAEMAGLLRE ELEALGLETR VVRVPDEVVE KHYPWARGYP
RFIVLARLGE GRPVLHLNGH YDVVPPGQGW ARDPFNPVVE NGRVYGRGAT DMKGGIAAVI
AAIRGLVEEG WRPRRGSIEL SFTPDEETGG ETGVKYMLDE GLTLPDYALV AEPSTTSRIW
IGSRGAVWMN VHVYGRQAHG STPWLGLNAF EAMVEIAYRL IHGYKPRLAE RRTDLPMDDP
RAAHPTITIG GEIEGGAKTN VVPGYYRFSI DRRLIPGEDP DEVERELRDF IMESAAPLLE
KGYRVEVETT GKAPATWIPP DNPFVETVAE AVREALGLEP LRTICTGGLD TRYFQQRGIP
AVTYGPGAPG AAHKPDEYVP LEELENAVKV YRALIRRILG
//
