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Database: UniProt
Entry: A0A2T0LL29_9PSEU
LinkDB: A0A2T0LL29_9PSEU
Original site: A0A2T0LL29_9PSEU 
ID   A0A2T0LL29_9PSEU        Unreviewed;       420 AA.
AC   A0A2T0LL29;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:PRX43594.1};
GN   ORFNames=B0I33_11454 {ECO:0000313|EMBL:PRX43594.1};
OS   Prauserella shujinwangii.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=1453103 {ECO:0000313|EMBL:PRX43594.1, ECO:0000313|Proteomes:UP000238362};
RN   [1] {ECO:0000313|EMBL:PRX43594.1, ECO:0000313|Proteomes:UP000238362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7125 {ECO:0000313|EMBL:PRX43594.1,
RC   ECO:0000313|Proteomes:UP000238362};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) 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:PRX43594.1}.
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DR   EMBL; PVNH01000014; PRX43594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0LL29; -.
DR   OrthoDB; 9808195at2; -.
DR   Proteomes; UP000238362; 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 AMIDOHYDROLASE; 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:PRX43594.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238362};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         232
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         291
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         304
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   420 AA;  42971 MW;  AEC63B4584B39345 CRC64;
     MTGAGSEGHL HCVQRSEGGL HCPSASALLA EIADIGCDRR RGGYSRHVFD GAERELRGWF
     ADHAARLGLD TETDRNGNVW AWWGTPGPGA VVTGSHLDSV PGGGAFDGPL GVASALTAVG
     ALRARGGTPA RPLAVVVFAE EEGGRFGVPC LGSRLLTGAI DAEAARNLRD PEGVTFAEAA
     RAAGLDPARI GPDPEALGRI GTFVELHVEQ GRGLIDLGSP VAVGSTVIAH GRWRFTFTGQ
     GNHAGATPLS DRRDPMLPAA ATVAAVRRLA AGVPDARATV GRLVPSPGGT NVIASTVDLW
     LDARVPGGGT QALVDDITAA ARAAAADEGC ALTVRQESCS DTVAFDDRLR AELGGLLGGV
     PELATGAGHD AAILAPHVPS AMLYVRNPTG VSHAPEEHAE PADVERGAAA LTDVLEHLCR
//
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