ID B6YR22_AZOPC Unreviewed; 351 AA.
AC B6YR22;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN OrderedLocusNames=CFPG_381 {ECO:0000313|EMBL:BAG83644.1};
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995 {ECO:0000313|EMBL:BAG83644.1, ECO:0000313|Proteomes:UP000000723};
RN [1] {ECO:0000313|Proteomes:UP000000723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
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; AP010656; BAG83644.1; -; Genomic_DNA.
DR RefSeq; WP_012573405.1; NC_011565.1.
DR AlphaFoldDB; B6YR22; -.
DR STRING; 511995.CFPG_381; -.
DR KEGG; aps:CFPG_381; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_10; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000000723; 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:UP000000723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 166..260
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 351 AA; 39410 MW; B90FAC66D7BF8866 CRC64;
MFPPTNKALN LLKKLISIPS FSREETEAAN WLEFFLIKEN FRPKRKGNNI WVLSDKWDDT
KPTILLNSHI DTVKPVYSWT KNPFSPLEEN KKLYGLGSND AGASLVALLQ SFFILTSRWQ
PNNFIFLVSC EEEVSGSEGL GSVLTELPPI TLAVVGEPTE MQPAVAERGL MVLDGTVYGK
SGHAARDEGI NAIYKAIPII NWFQNLQFPL KSDWLGSVKS TITMIQSGMQ HNIIPDICQF
TVDIRSNECY TNKQLFEEII RTSPCEIKAR SLRLNSSQIS LDNPLIRRAK SFGLKPFGSL
TLSDQALMNF PSLKIGPGDS SRSHIADEFV YLSEIEEAIK LYFCLLNNLT L
//
