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
//