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Protein

Allantoate amidohydrolase

Gene

allC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the anaerobic utilization of allantoin. Converts allantoate to (S)-ureidoglycolate and ammonia.1 Publication

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Pathwayi: (S)-allantoin degradation

This protein is involved in the pathway (S)-allantoin degradation, which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway (S)-allantoin degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Zinc 1
Metal bindingi92 – 921Zinc 1
Metal bindingi92 – 921Zinc 2
Metal bindingi127 – 1271Zinc 2
Metal bindingi190 – 1901Zinc 1
Metal bindingi382 – 3821Zinc 2

GO - Molecular functioni

  • allantoate deiminase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc

GO - Biological processi

  • allantoin assimilation pathway Source: EcoCyc
  • purine nucleobase metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G6285-MONOMER.
ECOL316407:JW0504-MONOMER.
MetaCyc:G6285-MONOMER.
BRENDAi3.5.3.9. 2026.
UniPathwayiUPA00395.

Protein family/group databases

MEROPSiM20.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Allantoate amidohydrolase (EC:3.5.3.-)
Alternative name(s):
Allantoate deiminase
Gene namesi
Name:allC
Synonyms:glxB7, ylbB
Ordered Locus Names:b0516, JW0504
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13623. allC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Allantoate amidohydrolasePRO_0000061957Add
BLAST

Proteomic databases

PaxDbiP77425.
PRIDEiP77425.

Expressioni

Inductioni

By glyoxylate and allantoin under anaerobic conditions.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4261167. 17 interactions.
DIPiDIP-9088N.
IntActiP77425. 9 interactions.
STRINGi511145.b0516.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1817Combined sources
Beta strandi25 – 273Combined sources
Helixi34 – 4916Combined sources
Beta strandi53 – 564Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 8113Combined sources
Helixi94 – 11118Combined sources
Beta strandi115 – 12410Combined sources
Beta strandi130 – 1323Combined sources
Helixi136 – 1416Combined sources
Helixi147 – 1493Combined sources
Turni150 – 1523Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1677Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi193 – 1953Combined sources
Helixi196 – 1994Combined sources
Beta strandi203 – 2108Combined sources
Beta strandi212 – 22110Combined sources
Turni227 – 2293Combined sources
Helixi232 – 2343Combined sources
Helixi238 – 25619Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi279 – 29113Combined sources
Helixi292 – 31322Combined sources
Beta strandi316 – 32510Combined sources
Helixi332 – 34413Combined sources
Beta strandi349 – 3568Combined sources
Helixi359 – 3635Combined sources
Turni364 – 3663Combined sources
Beta strandi369 – 3746Combined sources
Helixi377 – 3793Combined sources
Helixi390 – 40819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2LX-ray2.25A/B2-411[»]
2IMOX-ray2.80A/B2-411[»]
4PXDX-ray2.20A/B1-411[»]
ProteinModelPortaliP77425.
SMRiP77425. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77425.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20 family.Curated

Phylogenomic databases

eggNOGiENOG4105CE7. Bacteria.
COG0624. LUCA.
HOGENOMiHOG000241291.
InParanoidiP77425.
KOiK02083.
OMAiVKFHPDC.
OrthoDBiEOG6MH5CS.
PhylomeDBiP77425.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR017591. Allantoate_amidohydrolase.
IPR010158. Amidase_hdtase/Cbmase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF001235. Amidase_carbamoylase. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR03176. AllC. 1 hit.
TIGR01879. hydantase. 1 hit.

Sequencei

Sequence statusi: Complete.

P77425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITHFRQAIE ETLPWLSSFG ADPAGGMTRL LYSPEWLETQ QQFKKRMAAS
60 70 80 90 100
GLETRFDEVG NLYGRLNGTE YPQEVVLSGS HIDTVVNGGN LDGQFGALAA
110 120 130 140 150
WLAIDWLKTQ YGAPLRTVEV VAMAEEEGSR FPYVFWGSKN IFGLANPDDV
160 170 180 190 200
RNICDAKGNS FVDAMKACGF TLPNAPLTPR QDIKAFVELH IEQGCVLESN
210 220 230 240 250
GQSIGVVNAI VGQRRYTVTL NGESNHAGTT PMGYRRDTVY AFSRICHQSV
260 270 280 290 300
EKAKRMGDPL VLTFGKVEPR PNTVNVVPGK TTFTIDCRHT DAAVLRDFTQ
310 320 330 340 350
QLENDMRAIC DEMDIGIDID LWMDEEPVPM NKELVATLTE LCEREKLNYR
360 370 380 390 400
VMHSGAGHDA QIFAPRVPTC MIFIPSINGI SHNPAERTNI TDLAEGVKTL
410
ALMLYQLAWQ K
Length:411
Mass (Da):45,694
Last modified:February 1, 1997 - v1
Checksum:iC55D1EF854A8F513
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89279 Genomic DNA. Translation: AAB93857.1.
U82664 Genomic DNA. Translation: AAB40268.1.
U00096 Genomic DNA. Translation: AAC73618.1.
AP009048 Genomic DNA. Translation: BAE76294.1.
PIRiC64783.
RefSeqiNP_415049.1. NC_000913.3.
WP_001310618.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73618; AAC73618; b0516.
BAE76294; BAE76294; BAE76294.
GeneIDi945150.
KEGGiecj:JW0504.
eco:b0516.
PATRICi32116189. VBIEscCol129921_0536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89279 Genomic DNA. Translation: AAB93857.1.
U82664 Genomic DNA. Translation: AAB40268.1.
U00096 Genomic DNA. Translation: AAC73618.1.
AP009048 Genomic DNA. Translation: BAE76294.1.
PIRiC64783.
RefSeqiNP_415049.1. NC_000913.3.
WP_001310618.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2LX-ray2.25A/B2-411[»]
2IMOX-ray2.80A/B2-411[»]
4PXDX-ray2.20A/B1-411[»]
ProteinModelPortaliP77425.
SMRiP77425. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261167. 17 interactions.
DIPiDIP-9088N.
IntActiP77425. 9 interactions.
STRINGi511145.b0516.

Protein family/group databases

MEROPSiM20.976.

Proteomic databases

PaxDbiP77425.
PRIDEiP77425.

Protocols and materials databases

DNASUi945150.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73618; AAC73618; b0516.
BAE76294; BAE76294; BAE76294.
GeneIDi945150.
KEGGiecj:JW0504.
eco:b0516.
PATRICi32116189. VBIEscCol129921_0536.

Organism-specific databases

EchoBASEiEB3388.
EcoGeneiEG13623. allC.

Phylogenomic databases

eggNOGiENOG4105CE7. Bacteria.
COG0624. LUCA.
HOGENOMiHOG000241291.
InParanoidiP77425.
KOiK02083.
OMAiVKFHPDC.
OrthoDBiEOG6MH5CS.
PhylomeDBiP77425.

Enzyme and pathway databases

UniPathwayiUPA00395.
BioCyciEcoCyc:G6285-MONOMER.
ECOL316407:JW0504-MONOMER.
MetaCyc:G6285-MONOMER.
BRENDAi3.5.3.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP77425.
PROiP77425.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR017591. Allantoate_amidohydrolase.
IPR010158. Amidase_hdtase/Cbmase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF001235. Amidase_carbamoylase. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR03176. AllC. 1 hit.
TIGR01879. hydantase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli."
    Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.
    J. Bacteriol. 181:7479-7484(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: K12 / ECL1.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Crystal structure of allantoate-amidohydrolase from E.coli K12 in complex with substrate allantoate."
    New York structural genomix research consortium (NYSGXRC)
    Submitted (MAR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-411.
  6. "Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics."
    Agarwal R., Burley S.K., Swaminathan S.
    J. Mol. Biol. 368:450-463(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiALLC_ECOLI
AccessioniPrimary (citable) accession number: P77425
Secondary accession number(s): Q2MBR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.