ID   G0HH08_CORVD            Unreviewed;       468 AA.
AC   G0HH08;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Putative amidohydrolase {ECO:0000313|EMBL:AEK37996.1};
GN   OrderedLocusNames=CVAR_2655 {ECO:0000313|EMBL:AEK37996.1};
OS   Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS   NCIMB 30131) (Corynebacterium mooreparkense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK37996.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK37996.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT   from the surface of smear-ripened cheeses and insights into cheese ripening
RT   and flavor generation.";
RL   BMC Genomics 12:545-545(2011).
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DR   EMBL; CP002917; AEK37996.1; -; Genomic_DNA.
DR   RefSeq; WP_014011147.1; NC_015859.1.
DR   AlphaFoldDB; G0HH08; -.
DR   STRING; 858619.CVAR_2655; -.
DR   KEGG; cva:CVAR_2655; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_2_3_11; -.
DR   Proteomes; UP000006659; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AEK37996.1}.
FT   DOMAIN          60..425
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   468 AA;  50108 MW;  8E72B9859E6FE95F CRC64;
     MSTLFIDAVI IPVDPAQPRW FRGWLSVDDD GRITGLGEGT PDPATTAAFS EVVDLNGAFL
     APGFISAHSH IYTGGMRGIA HTEPLYTWVT QNSAMLAEAD PEIMYWLSRA GGLDHLAAGV
     TSVYNFTQSR VVCRFDYASS TLKAVKVHDP DFVTRQIDGV ADAGIRFVTS VRVDDEQLPE
     ADAVAGFDAA MSHLTTIDAK TPALNLGGSV YGAVQWASGR RTAELEKELM EKWSITNQAH
     FVETAEQIEI QQAKFDWYDD AGVLGTDFAF GHFVHPTERM VERVVESGTS VVWQAMSNGR
     LGSGIADITG LLAKDVTVGM GVDDQSCTDT SDPFENMRTG LFTQRAVHSD ASIMSVDQVL
     HLHTLGSASS IGVADKVGSL TVGKYADLVV VDPRHPATGP VWDPVATYVL ACGLRHLRRV
     YVGGKVAFDA DLPGGVTGAD GVTYDEVNRA ADEGMVRSAV AGGFTPAY
//