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Database: UniProt
Entry: D9XWQ8_9ACTN
LinkDB: D9XWQ8_9ACTN
Original site: D9XWQ8_9ACTN 
ID   D9XWQ8_9ACTN            Unreviewed;       409 AA.
AC   D9XWQ8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=N-carbamoyl-L-amino acid hydrolase {ECO:0000313|EMBL:EFL40987.1};
GN   ORFNames=SSRG_03791 {ECO:0000313|EMBL:EFL40987.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL40987.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL40987.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL40987.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) 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; GG657758; EFL40987.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XWQ8; -.
DR   STRING; 467200.SSRG_03791; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_024588_6_0_11; -.
DR   Proteomes; UP000002968; 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   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   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:EFL40987.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         215
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         273
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         286
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   409 AA;  43512 MW;  745D5CB68B480D08 CRC64;
     MRPGGGFLGM WRQLARIGRS SESGGYRRFA WGGADAECRE WFEEQVRARG LAYEVDRNGN
     QWGWLGDPAR GDAVVTGSHL DSVPDGGAFD GPLGVVSAFA ALDELLRRGA RLTKPLGVVN
     FGDEEGARFG LACVGSRLTA GALTVEQAHR LTDADGITLP QAMEAAGHDP GTLGPDPERL
     DRIGAFVELH VEQGRALDLS GDRVGIASAI WPHGRWRFDF RGEANHAGTT RLTDRRDPML
     SYAETVLAAR REAELAGAVA TFGKIAVEPN GVNAIPSLVR GWLDSRAADQ ESLDTVVEGV
     RKAARDHARQ HGVTLDVERE SFTPVVEFDH ALRDELARIL AGDTGRAVPV LGTGAGHDAG
     ILSGRVPTAM LFVRNPTGVS HSPAEYATED DCVAGVTALA DVLEGLACT
//
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