ALLB_ECOLI
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 03-AUG-2022, entry version 161.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=17.0 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=80.0 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 zinc-
CC 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_SSZK01000024.1.
DR PDB; 3E74; X-ray; 2.10 A; A/B/C/D=1-453.
DR PDBsum; 3E74; -.
DR AlphaFoldDB; P77671; -.
DR SMR; P77671; -.
DR BioGRID; 4259862; 12.
DR IntAct; P77671; 7.
DR STRING; 511145.b0512; -.
DR PaxDb; P77671; -.
DR PRIDE; P77671; -.
DR EnsemblBacteria; AAC73614; AAC73614; b0512.
DR EnsemblBacteria; BAE76290; BAE76290; BAE76290.
DR GeneID; 945134; -.
DR KEGG; ecj:JW0500; -.
DR KEGG; eco:b0512; -.
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; WVTAEVT; -.
DR PhylomeDB; P77671; -.
DR BioCyc; EcoCyc:G6281-MON; -.
DR BioCyc; MetaCyc:G6281-MON; -.
DR BRENDA; 3.5.2.5; 2026.
DR SABIO-RK; P77671; -.
DR UniPathway; UPA00395; UER00653.
DR EvolutionaryTrace; P77671; -.
DR PRO; PR:P77671; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0009442; P:allantoin assimilation pathway; IDA:EcoCyc.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR Gene3D; 2.30.40.10; -; 1.
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 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:3E74"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 217..234
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:3E74"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 412..415
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:3E74"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:3E74"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:3E74"
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
