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Database: UniProt
Entry: A7H181_CAMC5
LinkDB: A7H181_CAMC5
Original site: A7H181_CAMC5 
ID   A7H181_CAMC5            Unreviewed;       411 AA.
AC   A7H181;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   SubName: Full=Peptidase family M20/M25/M40, putative N-carbamoyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:EAU00814.1};
GN   ORFNames=CCV52592_2070 {ECO:0000313|EMBL:EAU00814.1};
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU00814.1, ECO:0000313|Proteomes:UP000006380};
RN   [1] {ECO:0000313|Proteomes:UP000006380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC       1};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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DR   EMBL; CP000767; EAU00814.1; -; Genomic_DNA.
DR   RefSeq; WP_011992902.1; NC_009715.2.
DR   AlphaFoldDB; A7H181; -.
DR   STRING; 360105.CCV52592_2070; -.
DR   KEGG; ccv:CCV52592_2070; -.
DR   HOGENOM; CLU_024588_6_0_7; -.
DR   OMA; IWPHGRW; -.
DR   OrthoDB; 9808195at2; -.
DR   Proteomes; UP000006380; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE AMIDOHYDROLASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          216..310
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         216
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         275
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         288
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   411 AA;  44798 MW;  92A490684D3332F0 CRC64;
     MINRKRLQGE FEAISKFGAL ESGGLTRLAF TKEDKQAREY LISLVKEAGF SLKEDAVGNI
     YAKFDDVSEP NLPAVSVGSH VDSVPFGGFY DGTLGVMTGL EAMRAIKESG VKLKRPIELI
     VFCCEESSRF KMATIGSKIV SGKLPLSRLH ELKDESGVSL YDAMRDFGLK PQNLADALLP
     KGAFHSYLEL HIEQGPVLER QNIPIGIVTG IAAPIRYEIL VRGRADHSGA TPMNMRNDAL
     VAASHIIIAA QNFARAKKTA VATIGYAQTK PGVLNVVPGE VRLGVDIRDI DKSDLEALDK
     ELRAFVQELS GELNFSYEIK ELIKDMPMRL SDEVINLLEN EAKSLGIKTL RLPSGAGHDA
     MNMPGIAKLV GMLFIPCKDG ISHNINESIN FDDAFKATEI LAAAMIKLSQ N
//
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