ID   ALLB_ECOLI              Reviewed;         453 AA.
AC   P77671; Q2MBR6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 178.
DE   RecName: Full=Allantoinase;
DE            EC=3.5.2.5;
DE   AltName: Full=Allantoin-utilizing enzyme;
GN   Name=allB; Synonyms=glxB3, ybbX; OrderedLocusNames=b0512, JW0500;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12 / ECL1;
RX   PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA   Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT   "Genetic analysis of a chromosomal region containing genes required for
RT   assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT   Escherichia coli.";
RL   J. Bacteriol. 181:7479-7484(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF N-TERMINUS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, COFACTOR, ACTIVITY REGULATION, FUNCTION, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=11092864; DOI=10.1128/jb.182.24.7021-7028.2000;
RA   Kim G.J., Lee D.E., Kim H.-S.;
RT   "Functional expression and characterization of the two cyclic
RT   amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from
RT   Escherichia coli.";
RL   J. Bacteriol. 182:7021-7028(2000).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, STEREOSPECIFICITY, AND
RP   COFACTOR.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=12486048; DOI=10.1128/jb.185.1.126-134.2003;
RA   Mulrooney S.B., Hausinger R.P.;
RT   "Metal ion dependence of recombinant Escherichia coli allantoinase.";
RL   J. Bacteriol. 185:126-134(2003).
CC   -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC       allantoic acid by hydrolytic cleavage of the five-member hydantoin
CC       ring. {ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:11092864}.
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;
CC         Evidence={ECO:0000269|PubMed:11092864};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048,
CC         ECO:0000305};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048,
CC         ECO:0000305};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048,
CC         ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048,
CC         ECO:0000305};
CC       Note=Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or
CC       Mn(2+). {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048,
CC       ECO:0000305};
CC   -!- ACTIVITY REGULATION: Severely inhibited by copper, and competitively
CC       inhibited by dithiothreitol (DTT). Zinc concentrations above 2.5 mM and
CC       cobalt or nickel concentrations above 1 mM are inhibitors.
CC       {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.2 mM for allantoin (at 40 degrees Celsius and pH 8.0)
CC         {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048};
CC         KM=17 mM for allantoin (in zinc-supplemented medium at 37 degrees
CC         Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         KM=19.5 mM for allantoin (in cobalt-supplemented medium at 37 degrees
CC         Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         KM=80 mM for allantoin (in nickel-supplemented medium at 37 degrees
CC         Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         Vmax=101 umol/min/mg enzyme (in zinc-supplemented medium at 37
CC         degrees Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         Vmax=8.1 umol/min/mg enzyme (in cobalt-supplemented medium (20mM) at
CC         37 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         Vmax=6.7 umol/min/mg enzyme (at 40 degrees Celsius and pH 8.0)
CC         {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048};
CC         Vmax=3.9 umol/min/mg enzyme (in cobalt-supplemented medium (2mM) at
CC         37 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC         Vmax=0.7 umol/min/mg enzyme (without added metal at 37 degrees
CC         Celsius and pH 7.4) {ECO:0000269|PubMed:11092864,
CC         ECO:0000269|PubMed:12486048};
CC       pH dependence:
CC         Optimum pH is 7.5-8.0. The optimal activity is at pH 8.8 for
CC         zinc-containing form and pH 9.0 for cobalt-containing form.
CC         {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048};
CC       Temperature dependence:
CC         Optimum temperature is 40-45 degrees Celsius.
CC         {ECO:0000269|PubMed:11092864, ECO:0000269|PubMed:12486048};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC       from (S)-allantoin: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11092864}.
CC   -!- INDUCTION: By glyoxylate.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: The zinc-containing form utilizes only the (S)-isomer of
CC       allantoin, whereas the cobalt-containing form prefers the (S)-isomer,
CC       but also hydrolyzes the (R)-isomer at about 1/10 the rate.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Allantoinase family. {ECO:0000305}.
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DR   EMBL; U89279; AAB93853.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40264.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73614.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76290.1; -; Genomic_DNA.
DR   PIR; G64782; G64782.
DR   RefSeq; NP_415045.1; NC_000913.3.
DR   RefSeq; WP_000006900.1; NZ_CP009789.1.
DR   PDB; 3E74; X-ray; 2.10 A; A/B/C/D=1-453.
DR   PDB; 8HFD; X-ray; 2.07 A; A/B/C/D=1-453.
DR   AlphaFoldDB; P77671; -.
DR   SMR; P77671; -.
DR   BioGRID; 4259862; 19.
DR   FunCoup; P77671; 834.
DR   IntAct; P77671; 7.
DR   STRING; 511145.b0512; -.
DR   PaxDb; 511145-b0512; -.
DR   EnsemblBacteria; AAC73614; AAC73614; b0512.
DR   GeneID; 945134; -.
DR   KEGG; ecj:JW0500; -.
DR   KEGG; eco:b0512; -.
DR   KEGG; ecoc:C3026_02510; -.
DR   PATRIC; fig|1411691.4.peg.1766; -.
DR   EchoBASE; EB3384; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_4_2_6; -.
DR   InParanoid; P77671; -.
DR   OMA; AADCHYH; -.
DR   OrthoDB; 5687299at2; -.
DR   PhylomeDB; P77671; -.
DR   BioCyc; EcoCyc:G6281-MONOMER; -.
DR   BioCyc; MetaCyc:G6281-MONOMER; -.
DR   BRENDA; 3.5.2.5; 2026.
DR   SABIO-RK; P77671; -.
DR   UniPathway; UPA00395; UER00653.
DR   EvolutionaryTrace; P77671; -.
DR   PRO; PR:P77671; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P77671; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0004038; F:allantoinase activity; IDA:EcoliWiki.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
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   FunFam; 3.20.20.140:FF:000013; Allantoinase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   HAMAP; MF_01645; Hydantoinase; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR047604; Allantoinase_bact.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR050138; DHOase/Allantoinase_Hydrolase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03178; allantoinase; 1.
DR   NCBIfam; NF005960; allB; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF4; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Purine metabolism; Reference proteome; Zinc.
FT   CHAIN           1..453
FT                   /note="Allantoinase"
FT                   /id="PRO_0000165942"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         146
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           73..82
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           102..112
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           134..140
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           190..202
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           208..213
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           217..234
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           246..257
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           275..281
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           294..305
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           321..324
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   TURN            328..330
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           338..340
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           342..345
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           346..351
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           357..361
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           362..366
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           367..371
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          388..394
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   TURN            412..415
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          417..419
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          421..427
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   TURN            435..437
FT                   /evidence="ECO:0007829|PDB:8HFD"
FT   HELIX           450..452
FT                   /evidence="ECO:0007829|PDB:8HFD"
SQ   SEQUENCE   453 AA;  49602 MW;  5CFE588F94268AB4 CRC64;
     MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV VSPGMVDAHT
     HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA
     AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG
     QPVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV
     CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM
     WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF
     GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA
     RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ
//