ID A0A286IIN1_9BACT Unreviewed; 364 AA.
AC A0A286IIN1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN ORFNames=SAMN06298216_0907 {ECO:0000313|EMBL:SOE20413.1};
OS Spirosomataceae bacterium TFI 002.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE20413.1, ECO:0000313|Proteomes:UP000217493};
RN [1] {ECO:0000313|EMBL:SOE20413.1, ECO:0000313|Proteomes:UP000217493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFI 002 {ECO:0000313|EMBL:SOE20413.1,
RC ECO:0000313|Proteomes:UP000217493};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; LT907983; SOE20413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286IIN1; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000217493; Chromosome i.
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:UP000217493};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 170..264
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 364 AA; 40427 MW; FF46EE12C48ECE27 CRC64;
MLIDSQLTQD AISLLKKLIA TPSFSREESG TAAILEEHFR ERNIPYSKQD HNVWARNQFF
NKELPTILLN SHHDTVKPNA GYTKNPHEPI EEDGKLYGLG SNDAGGPLVC LIAVFEHYYY
RSDLSFNLVL AASAEEEVSG KNGIEALIPN LPKIDLAIVG EPTLLKIAVS EKGLMVIDAE
VKGIAGHAAR EEGENAIFKA IQDLEWFKNY EYPLVSDSLG KMKQSVTVCS AGTQHNVVPD
LFKYTVDVRM TDAYTMEEVL QIIDQNTVAS IKPRSTRLKP SGLPKGHYIY GIAENLKIDT
YGSPTLSDQA LMPFQSIKMG PGDSARSHSA DEFIYLDEIK YGIEAYVALL KAIHKHFKNN
DLEA
//
