ID F4KPH2_HALH1 Unreviewed; 350 AA.
AC F4KPH2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN OrderedLocusNames=Halhy_2041 {ECO:0000313|EMBL:AEE49926.1};
OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Haliscomenobacter.
OX NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE49926.1, ECO:0000313|Proteomes:UP000008461};
RN [1] {ECO:0000313|EMBL:AEE49926.1, ECO:0000313|Proteomes:UP000008461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC {ECO:0000313|Proteomes:UP000008461};
RX PubMed=21886862; DOI=10.4056/sigs.1964579;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL Stand. Genomic Sci. 4:352-360(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1100;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00001246};
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; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}.
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DR EMBL; CP002691; AEE49926.1; -; Genomic_DNA.
DR RefSeq; WP_013764479.1; NC_015510.1.
DR AlphaFoldDB; F4KPH2; -.
DR STRING; 760192.Halhy_2041; -.
DR GeneID; 78191933; -.
DR KEGG; hhy:Halhy_2041; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_10; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000008461; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05651; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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 PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008461};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 166..268
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 350 AA; 38530 MW; F0D8706DBC601A3D CRC64;
MSVADSAIDL LKILIATPSF SKEEDEAAQQ VAIFLTKRYI PFTRKGNNIW ARNRHWQNGK
PILLLNSHMD TVKPATGWQR DPFHPGIEAE DVLYGLGSND AGGPLVALIA TFLHFYERED
LPVNIIMAAT AEEEISGAQG IASVIPELGP VDFAIVGEPT QMKMAIAEKG LMVVDGEAKG
VSGHAAREEG INALYIALED IERIRRMDLE RVSPLLGKVK MTVTQIEAGK QHNVVPDSCR
FVIDVRTNEC YRNEEVFEIL QSQLQSELTP RSFRLNSSGI ALEHPLVQSG LNLGLPYFGS
PTLSDQALMP FPSLKIGPGD SARSHTADEY IRLSEIRAGI DTYIRLIEGI
//
