ID   Y1398_METMP             Reviewed;         415 AA.
AC   Q6LXF3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Uncharacterized metallohydrolase MMP1398;
DE            EC=3.-.-.-;
GN   OrderedLocusNames=MMP1398;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   LACK OF FUNCTION AS A SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE.
RX   PubMed=18371309; DOI=10.1016/j.febslet.2008.03.021;
RA   Graham D.E., Huse H.K.;
RT   "Methanogens with pseudomurein use diaminopimelate aminotransferase in
RT   lysine biosynthesis.";
RL   FEBS Lett. 582:1369-1374(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC   -!- CAUTION: Despite its similarity with the succinyl-diaminopimelate
CC       desuccinylase enzymes, it does not display DapE activity.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX950229; CAF30954.1; -; Genomic_DNA.
DR   RefSeq; WP_011171342.1; NC_005791.1.
DR   AlphaFoldDB; Q6LXF3; -.
DR   SMR; Q6LXF3; -.
DR   STRING; 267377.MMP1398; -.
DR   EnsemblBacteria; CAF30954; CAF30954; MMP1398.
DR   GeneID; 2761514; -.
DR   KEGG; mmp:MMP1398; -.
DR   PATRIC; fig|267377.15.peg.1434; -.
DR   eggNOG; arCOG01107; Archaea.
DR   HOGENOM; CLU_021802_2_2_2; -.
DR   OMA; STFEPTM; -.
DR   OrthoDB; 14646at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07195-MON; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR010182; ArgE/DapE.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01910; DapE-ArgE; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..415
FT                   /note="Uncharacterized metallohydrolase MMP1398"
FT                   /id="PRO_0000342209"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  46968 MW;  B50D0D2E9C6EACD8 CRC64;
     MKSILDETIE LSSDLISINS VNPTFGGIGE KEKSIYIKNK LEEYNKNYSI KNCEITEYNT
     VDSEGIERPN IVSKYDFGKN DTLTIISHMD IVPEGDLGLW NSDPFKAEIK DGIIYGRGSE
     DNHKGIVSSF LLLKMIFEEK IDPKYNLNLI FVADEEDGSK YGLSYLVNNF EDEIFSSKDL
     IIVPDFGMPE GEFIEIAEKN ILWLKFKITG KQCHGSVPEN GINADLIAFS FGKGLYDKLY
     GKYDGINPIF NPAFSTFEPT ILKNNIENIN TIPGYVELNF DCRIIPKYDP KEVLSDIENY
     IEVFKNEIEK HILHFDISEK ENISITYEIL KLEKAEETKK DSEVVKKLGS AIKNVLNKES
     VLCGMGGGTV AAFLREKGYN TAVWGIGDET AHQPNEHIKI ENLIKMAEVY LDILK