ID F8KTB8_HELBC Unreviewed; 377 AA.
AC F8KTB8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00022391};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000256|ARBA:ARBA00031891};
GN OrderedLocusNames=HBZC1_10830 {ECO:0000313|EMBL:CCB80069.1};
OS Helicobacter bizzozeronii (strain CIII-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB80069.1, ECO:0000313|Proteomes:UP000008387};
RN [1] {ECO:0000313|EMBL:CCB80069.1, ECO:0000313|Proteomes:UP000008387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIII-1 {ECO:0000313|EMBL:CCB80069.1,
RC ECO:0000313|Proteomes:UP000008387};
RX PubMed=21705603; DOI=10.1128/JB.05439-11;
RA Schott T., Rossi M., Hanninen M.L.;
RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT from human gastric mucosa.";
RL J. Bacteriol. 193:4565-4566(2011).
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=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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC {ECO:0000256|ARBA:ARBA00006746}.
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DR EMBL; FR871757; CCB80069.1; -; Genomic_DNA.
DR RefSeq; WP_013890503.1; NC_015674.1.
DR AlphaFoldDB; F8KTB8; -.
DR STRING; 1002804.HBZC1_10830; -.
DR KEGG; hbi:HBZC1_10830; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_4_0_7; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000008387; 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:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR HAMAP; MF_01690; DapE; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR005941; DapE_proteobac.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01246; dapE_proteo; 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:ARBA00022605};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCB80069.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008387};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 177..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 377 AA; 41419 MW; 6C464DC755782F5F CRC64;
MNPLNVVWLA RELITFKTIT PQEEGIFDFI QSLFPGFEVV RADKEGVKNL FLYKRLGACD
NPLHFCFAGH IDVVPAGEGW SVDPFGGVIE DGFLYGRGAQ DMKGGVAALL CAVHDFCKQE
NPPNAIISIL LTSDEEGEAL YGTQYMLEVL QEQNLLPHFA LVAEPTSAET LGDSVKIGRR
GSISGQIVVN GICGHVAYPK TCLNPIDLIA DKLMLISGAL LDKGDDFFAP SKLVITTLKS
VSQASNVTPK TLEIRFNVRN SPLTSAEYIQ EFLDTILAKV PCDIELITNS KPFLSSQDSP
LAMQIKRAIL ETLQITPEFN TKGGTSDARF LRAFGVEVVE FGLLNDRIHA LNERVALGDL
EKLQQVFLRL LHLVLKD
//
