ID   ALLB_STRCO              Reviewed;         445 AA.
AC   Q9RKU5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Allantoinase {ECO:0000255|HAMAP-Rule:MF_01645};
DE            EC=3.5.2.5 {ECO:0000255|HAMAP-Rule:MF_01645};
DE   AltName: Full=Allantoin-utilizing enzyme {ECO:0000255|HAMAP-Rule:MF_01645};
GN   Name=allB {ECO:0000255|HAMAP-Rule:MF_01645};
GN   OrderedLocusNames=SCO6247; ORFNames=SCAH10.12, STAH10.12;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC       allantoic acid by hydrolytic cleavage of the five-member hydantoin
CC       ring. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-allantoin + H2O = allantoate + H(+); Xref=Rhea:RHEA:17029,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678,
CC         ChEBI:CHEBI:17536; EC=3.5.2.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01645};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01645};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01645};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC       from (S)-allantoin: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC       {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Allantoinase family. {ECO:0000255|HAMAP-Rule:MF_01645}.
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DR   EMBL; AL939126; CAB60166.1; -; Genomic_DNA.
DR   RefSeq; NP_630347.1; NC_003888.3.
DR   RefSeq; WP_003972680.1; NZ_VNID01000009.1.
DR   AlphaFoldDB; Q9RKU5; -.
DR   SMR; Q9RKU5; -.
DR   STRING; 100226.gene:17763906; -.
DR   PaxDb; 100226-SCO6247; -.
DR   PATRIC; fig|100226.15.peg.6361; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_4_0_11; -.
DR   InParanoid; Q9RKU5; -.
DR   OrthoDB; 9803027at2; -.
DR   PhylomeDB; Q9RKU5; -.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004038; F:allantoinase activity; IBA:GO_Central.
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:UniProtKB-UniRule.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR   CDD; cd01315; L-HYD_ALN; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   HAMAP; MF_01645; Hydantoinase; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR047604; Allantoinase_bact.
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   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT   CHAIN           1..445
FT                   /note="Allantoinase"
FT                   /id="PRO_0000165943"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   MOD_RES         150
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
SQ   SEQUENCE   445 AA;  47492 MW;  75955C5F98632570 CRC64;
     MSEAELVLRS TRVITPEGTR AASVAVTGEK ITAVLPYDAP VPAGARLEDV GDHVVLPGLV
     DTHVHVNDPG RTEWEGFWTA TRAAAAGGIT TLVDMPLNSI PPTTTVDNLR TKREVAADKA
     HIDVGFWGGA LPDNVKDLRP LHEAGVFGFK AFLSPSGVDE FPHLDQEQLA RSLAEIAAFD
     GLLIVHAEDP HHLAAAPQQG GPKYTHFLAS RPRDAEDTAI ATLLAQAKRF NARVHVLHLS
     SSDALPLIAE ARADGVRVTV ETCPHYLTLT AEEVPDGASE FKCCPPIREA ANQDLLWQAL
     ADGTIDCVVT DHSPSTADLK TDDFATAWGG IAGLQLSLPA MWTAARGRGL GLEDVVRWMS
     ERTAALVGLD ARKGAIAPGH DADFAVLAPD ETFTVDPAAL QHRNRVTAYA GKTLYGVVKS
     TWLRGERIVA DGAFTDPKGQ LLDRA
//