ID   Y994_METTH              Reviewed;         384 AA.
AC   O27075;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative aminohydrolase MTH_994;
DE            EC=3.-.-.-;
GN   OrderedLocusNames=MTH_994;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
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DR   EMBL; AE000666; AAB85491.1; -; Genomic_DNA.
DR   PIR; B69233; B69233.
DR   AlphaFoldDB; O27075; -.
DR   SMR; O27075; -.
DR   STRING; 187420.MTH_994; -.
DR   PRIDE; O27075; -.
DR   EnsemblBacteria; AAB85491; AAB85491; MTH_994.
DR   KEGG; mth:MTH_994; -.
DR   PATRIC; fig|187420.15.peg.977; -.
DR   HOGENOM; CLU_012358_1_0_2; -.
DR   OMA; TDNFMAN; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..384
FT                   /note="Putative aminohydrolase MTH_994"
FT                   /id="PRO_0000122312"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   384 AA;  42183 MW;  B534784121827933 CRC64;
     MNMLVVENGT ILRGPELTPQ RKNLVIEDGI IKEITDERAP SGERIDASKL MVCPALVNSH
     VHIGDSVALD VGDGRPLEDI VRPPNGLKHR ILESSPPGML MEAMRNSARD MITHGIGSFI
     DYREGGPEGV ELLREAIGDL PISGIILGRD PVVFDQEASR AEIRRRVRGV LRVSDGFAPS
     GMGEITDETA SIIVEECERA GKIASIHVAE HRESQRRSLE DTGMSEVERA LNAGFKLLVH
     LTNPVREDLK LVRESGASVV LCPRSNGALS SGIPPIRRMH ELGINLLLGT DNLMFNSPDM
     LREMEYTLKV TRGCARRYFP PVEVLRMATS NTSAFTGTGV IEEGFPADLI LVEKLSGDPY
     LSIINRTESK NIIYLIIKGK LVKR