ALLB_STRCO
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 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=SCO6247;
GN ORFNames=SCAH10.12, STAH10.12;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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;
CC Evidence={ECO:0000255|HAMAP-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.SCO6247; -.
DR PRIDE; Q9RKU5; -.
DR GeneID; 1101688; -.
DR KEGG; sco:SCO6247; -.
DR PATRIC; fig|100226.15.peg.6361; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_4_0_11; -.
DR InParanoid; Q9RKU5; -.
DR OMA; WVTAEVT; -.
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 HAMAP; MF_01645; Hydantoinase; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 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
