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P77425 (ALLC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Allantoate amidohydrolase

EC=3.5.3.-
Alternative name(s):
Allantoate deiminase
Gene names
Name:allC
Synonyms:glxB7, ylbB
Ordered Locus Names:b0516, JW0504
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

Binds 2 zinc ions per subunit.

Pathway

Nitrogen metabolism; (S)-allantoin degradation.

Subunit structure

Homodimer. Ref.6

Induction

By glyoxylate and allantoin under anaerobic conditions.

Sequence similarities

Belongs to the peptidase M20 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Allantoate amidohydrolase
PRO_0000061957

Sites

Metal binding831Zinc 1
Metal binding921Zinc 1
Metal binding921Zinc 2
Metal binding1271Zinc 2
Metal binding1901Zinc 1
Metal binding3821Zinc 2

Secondary structure

....................................................... 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77425 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C55D1EF854A8F513

FASTA41145,694
        10         20         30         40         50         60 
MITHFRQAIE ETLPWLSSFG ADPAGGMTRL LYSPEWLETQ QQFKKRMAAS GLETRFDEVG 

        70         80         90        100        110        120 
NLYGRLNGTE YPQEVVLSGS HIDTVVNGGN LDGQFGALAA WLAIDWLKTQ YGAPLRTVEV 

       130        140        150        160        170        180 
VAMAEEEGSR FPYVFWGSKN IFGLANPDDV RNICDAKGNS FVDAMKACGF TLPNAPLTPR 

       190        200        210        220        230        240 
QDIKAFVELH IEQGCVLESN GQSIGVVNAI VGQRRYTVTL NGESNHAGTT PMGYRRDTVY 

       250        260        270        280        290        300 
AFSRICHQSV EKAKRMGDPL VLTFGKVEPR PNTVNVVPGK TTFTIDCRHT DAAVLRDFTQ 

       310        320        330        340        350        360 
QLENDMRAIC DEMDIGIDID LWMDEEPVPM NKELVATLTE LCEREKLNYR VMHSGAGHDA 

       370        380        390        400        410 
QIFAPRVPTC MIFIPSINGI SHNPAERTNI TDLAEGVKTL ALMLYQLAWQ K 

« Hide

References

« Hide 'large scale' references
[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: 10601204] [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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 17362992] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89279 Genomic DNA. Translation: AAB93857.1.
U82664 Genomic DNA. Translation: AAB40268.1.
U00096 Genomic DNA. Translation: AAC73618.1.
AP009048 Genomic DNA. Translation: BAE76294.1.
PIRC64783.
RefSeqNP_415049.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2LX-ray2.25A/B2-411[»]
2IMOX-ray2.80A/B2-411[»]
ProteinModelPortalP77425.
SMRP77425. Positions 1-411.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9088N.
IntActP77425. 8 interactions.

Protein family/group databases

MEROPSM20.A13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000498; EBESCP00000000498; EBESCG00000000418.
EBESCT00000016128; EBESCP00000015419; EBESCG00000015188.
GeneID945150.
GenomeReviewsGene locus JW0504 in contig AP009048_GR.
Gene locus b0516 in contig U00096_GR.
KEGGecj:JW0504.
eco:b0516.
PATRIC32116189. VBIEscCol129921_0536.

Organism-specific databases

EchoBASEEB3388.
EcoGeneEG13623. allC.

Phylogenomic databases

eggNOGCOG0624.
GeneTreeEBGT00050000010235.
HOGENOMHBG583284.
OMAHRITHRI.
PhylomeDBP77425.
ProtClustDBPRK09290.

Enzyme and pathway databases

BioCycEcoCyc:G6285-MONOMER.
MetaCyc:G6285-MONOMER.

Gene expression databases

GenevestigatorP77425.

Family and domain databases

InterProIPR017591. Allantoate_amidohydrolase.
IPR010158. Amidase_hdtase/Cbmase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
KOK02083.
PfamPF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF001235. Amidase_carbamoylase. 1 hit.
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMsTIGR03176. AllC. 1 hit.
TIGR01879. Hydantase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLC_ECOLI
AccessionPrimary (citable) accession number: P77425
Secondary accession number(s): Q2MBR2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families