ID A0A0H2M501_VARPD Unreviewed; 418 AA.
AC A0A0H2M501;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:KLN57226.1};
DE EC=3.5.3.- {ECO:0000313|EMBL:KLN57226.1};
GN Name=allC {ECO:0000313|EMBL:KLN57226.1};
GN ORFNames=VPARA_13060 {ECO:0000313|EMBL:KLN57226.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN57226.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN57226.1, ECO:0000313|Proteomes:UP000035170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN57226.1,
RC ECO:0000313|Proteomes:UP000035170};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLN57226.1}.
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DR EMBL; JZWI01000007; KLN57226.1; -; Genomic_DNA.
DR RefSeq; WP_021003491.1; NZ_JZWI01000007.1.
DR AlphaFoldDB; A0A0H2M501; -.
DR PATRIC; fig|34073.19.peg.1330; -.
DR Proteomes; UP000035170; Unassembled WGS sequence.
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 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 NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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 Hydrolase {ECO:0000313|EMBL:KLN57226.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 418 AA; 45700 MW; C5C3D1EB4C592AFD CRC64;
MNVPGLQSIA EMLFSDVRDL SFDGIGVTRE SYGRGESATA EYLREFAKQQ GLDVHADRAA
NLVFRLPGSG ASPVVSWTGS HIDSVPQGGN FDGYAGVVAG LLCLLEQKRS GTRYRRPLEV
VAFRGEESAW FGKAYIGSGA LFGKISTADL DLKQRTTGQT MADCMLACGA DIEAIRTQQV
LIDRSRVKAY LELHIEQGPV MIARQLPLAV VSGIRGNVRH NRVVCHGDAQ HSGVVPRWLR
HDAMFAVADL IMRIDEHWRV LLERGTDLVV TTGIVTTDPS EHSISRIPGH VSFSLEARSK
STDTLEAFYQ LMRTECTAIE RERGVRFEFD RRLLSDPATM DTSICDVLSK ACSDQGTRFE
VIPSGAGHDA SLFANAGIPS GMLFVRNQNG SHNPHEAMDM GDFMLGVQAM HSSFAQLA
//
