ID A0A1W7D622_9ACTN Unreviewed; 395 AA.
AC A0A1W7D622;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:ARQ72434.1};
GN ORFNames=CAG99_17110 {ECO:0000313|EMBL:ARQ72434.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ72434.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ72434.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ72434.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-2017) 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; CP021121; ARQ72434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7D622; -.
DR KEGG; smao:CAG99_17110; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000194218; 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 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:ARQ72434.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194218};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 206
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 264
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 277
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 395 AA; 41477 MW; E69832739646A963 CRC64;
MWEELRPVGR EASTGGYRRY AWTAADGELR AWFRAQAARR GLRYEVDRNG NQWAWAGDPA
AGDAVVTGSH LDSVPDGGAF DGPLGVVSAF AALDVLRERG AVAARPVGVA GFADEEGARF
GVACLGSRLS CGLFDPDLAR GLRDADGVPL HRAMERAGLD PDAIGPDPER LAGIGAFVEL
HVEQGRALAG LGRPVGVGSV IRPHGRWRFD FRGRADHAGT TRIEDRRDPM LTYAHTVLAA
RKRARLAGAL ATFGKVDTEP NAVNAVPARV TAWLDCRADD PDALDALVAE IGRSAAERGE
RDGVSFALTR ESHTPGVAFA PGLRDDIAAR LGGAPVLPTG AGHDAGILAS AVPTAMLYVR
NPTGVSHAPD EHADEADCLA GVTALADVLE GMACR
//
