ID   A0A1W7D4W9_9ACTN        Unreviewed;       570 AA.
AC   A0A1W7D4W9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Allantoinase {ECO:0000313|EMBL:ARQ72128.1};
GN   ORFNames=CAG99_03170 {ECO:0000313|EMBL:ARQ72128.1};
OS   Streptomyces marincola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ72128.1, ECO:0000313|Proteomes:UP000194218};
RN   [1] {ECO:0000313|EMBL:ARQ72128.1, ECO:0000313|Proteomes:UP000194218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ72128.1,
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|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; CP021121; ARQ72128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W7D4W9; -.
DR   KEGG; smao:CAG99_03170; -.
DR   OrthoDB; 9803027at2; -.
DR   Proteomes; UP000194218; Chromosome.
DR   GO; GO:0004038; F:allantoinase activity; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03178; allantoinase; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194218}.
FT   DOMAIN          134..506
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  59086 MW;  FA7CA9FE7EAC96B0 CRC64;
     MCSSRAKARS KDWTPPPLAA VLRTSDGGTS RSFRAVKRQP TGPPLDVPRP SPEDRTRPFQ
     RNVEGRGVRG EAPGRRDGPL TATTLVLRST RVITPQGQRP ADIAVSGERI AAVLPHGSPP
     PAGARLVDYG DAALLPGLVD THVHVNDPGR TEWEGFATAT RAAAAGGVTT LVDMPLNSIP
     PTTTAAHLAV KRAVARDAVH TDVGFWGGAV PGNTADLRGL HEAGVFGFKC FLSPSGVEEF
     PELTPGGLEA AMTEIARLGA LLIVHAEDPG RLAEATPPAG SDRYADFLAS RPDAAETEAI
     ALLLALARRI GTRVHILHLS SAAALPLIAG ARAEGVRVTA ETCPHFLTLT AEEVPDGATE
     FKCCPPIREA ANQDLLWRAL AAGTLDAVVS DHSPCTADLK VPDFQAAWGG ISSLQLGLPV
     LWTAARARGH DLADVARWTA AGPARLAGLP DKGAIAPGRD ADIAVLDPEA EFTVDPAALH
     HRNPVTAYAG RTLRGVVRAT WLRGRRIAEH GNVIERAGGR LIVRHGTATD VPQARTADRD
     EAGGAGGGAG GAGGAPAAPA ARRDSGGGTP
//