ALLC_ECOLI
ID ALLC_ECOLI Reviewed; 411 AA.
AC P77425; Q2MBR2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Allantoate amidohydrolase {ECO:0000303|PubMed:10601204};
DE Short=AAH {ECO:0000303|PubMed:20038185};
DE EC=3.5.3.9 {ECO:0000269|PubMed:20038185};
DE AltName: Full=Allantoate deiminase {ECO:0000303|PubMed:17362992};
GN Name=allC {ECO:0000303|PubMed:10601204}; Synonyms=glxB7, ylbB;
GN OrderedLocusNames=b0516, JW0504;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND INDUCTION.
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20038185; DOI=10.1021/cb900248n;
RA Serventi F., Ramazzina I., Lamberto I., Puggioni V., Gatti R.,
RA Percudani R.;
RT "Chemical basis of nitrogen recovery through the ureide pathway: formation
RT and hydrolysis of S-ureidoglycine in plants and bacteria.";
RL ACS Chem. Biol. 5:203-214(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-411 IN COMPLEX WITH 2 ZINC IONS
RP AND ALLANTOATE, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=17362992; DOI=10.1016/j.jmb.2007.02.028;
RA Agarwal R., Burley S.K., Swaminathan S.;
RT "Structural analysis of a ternary complex of allantoate amidohydrolase from
RT Escherichia coli reveals its mechanics.";
RL J. Mol. Biol. 368:450-463(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT ALA-126 IN COMPLEX WITH
RP MANGANESE ION AND ALLANTOATE, MUTAGENESIS OF GLU-126, AND COFACTOR.
RX PubMed=25020232; DOI=10.1016/j.jmb.2014.06.017;
RA Shin I., Han K., Rhee S.;
RT "Structural insights into the substrate specificity of (s)-ureidoglycolate
RT amidohydrolase and its comparison with allantoate amidohydrolase.";
RL J. Mol. Biol. 426:3028-3040(2014).
CC -!- FUNCTION: Involved in the anaerobic nitrogen utilization via the
CC assimilation of allantoin (PubMed:10601204, PubMed:20038185). Catalyzes
CC specifically the hydrolysis of allantoate to yield CO2, NH3 and S-
CC ureidoglycine, which is unstable and readily undergoes a second
CC deamination by S-ureidoglycine aminohydrolase AllE to yield S-
CC ureidoglycolate and NH3 (PubMed:20038185). In vivo, the spontaneous
CC release of S-ureidoglycolate and ammonia from S-ureidoglycine appears
CC to be too slow to sustain an efficient flux of nitrogen
CC (PubMed:20038185). {ECO:0000269|PubMed:10601204,
CC ECO:0000269|PubMed:20038185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 +
CC NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59947; EC=3.5.3.9;
CC Evidence={ECO:0000269|PubMed:20038185};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17362992};
CC Note=Binds 2 Zn(2+) ions per subunit (PubMed:17362992). Also able to
CC bind Mn(2+) (PubMed:25020232). {ECO:0000269|PubMed:17362992,
CC ECO:0000269|PubMed:25020232};
CC -!- ACTIVITY REGULATION: Sulfate could be an allosteric effector of the
CC enzyme that is responsible for stabilizing substrate binding. In
CC addition, this anion effector may act as a counterion during enzyme-
CC mediated catalysis. {ECO:0000305|PubMed:17362992}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. Less active under acidic conditions.
CC {ECO:0000305|PubMed:17362992};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC {ECO:0000305|PubMed:10601204}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17362992}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By glyoxylate and allantoin under anaerobic conditions.
CC {ECO:0000269|PubMed:10601204}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; U89279; AAB93857.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40268.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73618.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76294.1; -; Genomic_DNA.
DR PIR; C64783; C64783.
DR RefSeq; NP_415049.1; NC_000913.3.
DR RefSeq; WP_001310618.1; NZ_SSZK01000024.1.
DR PDB; 1Z2L; X-ray; 2.25 A; A/B=2-411.
DR PDB; 2IMO; X-ray; 2.80 A; A/B=2-411.
DR PDB; 4PXD; X-ray; 2.20 A; A/B=1-411.
DR PDBsum; 1Z2L; -.
DR PDBsum; 2IMO; -.
DR PDBsum; 4PXD; -.
DR AlphaFoldDB; P77425; -.
DR SMR; P77425; -.
DR BioGRID; 4261167; 59.
DR BioGRID; 849538; 1.
DR DIP; DIP-9088N; -.
DR IntAct; P77425; 9.
DR STRING; 511145.b0516; -.
DR DrugBank; DB04380; Allantoate.
DR MEROPS; M20.976; -.
DR PaxDb; P77425; -.
DR PRIDE; P77425; -.
DR DNASU; 945150; -.
DR EnsemblBacteria; AAC73618; AAC73618; b0516.
DR EnsemblBacteria; BAE76294; BAE76294; BAE76294.
DR GeneID; 945150; -.
DR KEGG; ecj:JW0504; -.
DR KEGG; eco:b0516; -.
DR PATRIC; fig|1411691.4.peg.1762; -.
DR EchoBASE; EB3388; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_6; -.
DR InParanoid; P77425; -.
DR OMA; IWPHGRW; -.
DR PhylomeDB; P77425; -.
DR BioCyc; EcoCyc:G6285-MON; -.
DR BioCyc; MetaCyc:G6285-MON; -.
DR BRENDA; 3.5.3.4; 2026.
DR BRENDA; 3.5.3.9; 2026.
DR UniPathway; UPA00395; -.
DR EvolutionaryTrace; P77425; -.
DR PRO; PR:P77425; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047652; F:allantoate deiminase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009442; P:allantoin assimilation pathway; IDA:EcoCyc.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR017591; Allantoate_amidohydrolase.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR03176; AllC; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Purine metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..411
FT /note="Allantoate amidohydrolase"
FT /id="PRO_0000061957"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0007744|PDB:1Z2L"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0007744|PDB:1Z2L"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0000305|PubMed:25020232, ECO:0007744|PDB:1Z2L,
FT ECO:0007744|PDB:4PXD"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0000305|PubMed:25020232, ECO:0007744|PDB:1Z2L,
FT ECO:0007744|PDB:4PXD"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0007744|PDB:1Z2L"
FT BINDING 215
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0007744|PDB:1Z2L"
FT BINDING 275
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0000269|PubMed:25020232, ECO:0007744|PDB:1Z2L,
FT ECO:0007744|PDB:4PXD"
FT BINDING 288
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0000269|PubMed:25020232, ECO:0007744|PDB:1Z2L,
FT ECO:0007744|PDB:4PXD"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17362992,
FT ECO:0000305|PubMed:25020232, ECO:0007744|PDB:1Z2L,
FT ECO:0007744|PDB:4PXD"
FT MUTAGEN 126
FT /note="E->A: Loss of amidohydrolase activity. Large
FT movement of the catalytic domain into a closed
FT conformation."
FT /evidence="ECO:0000269|PubMed:25020232"
FT HELIX 2..18
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 69..81
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4PXD"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1Z2L"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2IMO"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:4PXD"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 238..256
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 292..313
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 316..325
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:4PXD"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:4PXD"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:4PXD"
FT HELIX 390..408
FT /evidence="ECO:0007829|PDB:4PXD"
SQ SEQUENCE 411 AA; 45694 MW; C55D1EF854A8F513 CRC64;
MITHFRQAIE ETLPWLSSFG ADPAGGMTRL LYSPEWLETQ QQFKKRMAAS GLETRFDEVG
NLYGRLNGTE YPQEVVLSGS HIDTVVNGGN LDGQFGALAA WLAIDWLKTQ YGAPLRTVEV
VAMAEEEGSR FPYVFWGSKN IFGLANPDDV RNICDAKGNS FVDAMKACGF TLPNAPLTPR
QDIKAFVELH IEQGCVLESN GQSIGVVNAI VGQRRYTVTL NGESNHAGTT PMGYRRDTVY
AFSRICHQSV EKAKRMGDPL VLTFGKVEPR PNTVNVVPGK TTFTIDCRHT DAAVLRDFTQ
QLENDMRAIC DEMDIGIDID LWMDEEPVPM NKELVATLTE LCEREKLNYR VMHSGAGHDA
QIFAPRVPTC MIFIPSINGI SHNPAERTNI TDLAEGVKTL ALMLYQLAWQ K
