Allantoate amidohydrolase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P77425 (ALLC_ECOLI)

Last modified June 16, 2009. Version 71. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Allantoate amidohydrolase
    EC=3.5.3.-
Alternative name(s):
    Allantoate deiminase

Gene names

Name:	allC
Synonyms:	glxB7, ylbB
Ordered Locus Names:	b0516, JW0504

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Purine metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro purine base metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 411

411

Allantoate amidohydrolase

PRO_0000061957

Sites

Metal binding

Zinc 1

Metal binding

Zinc 1

Metal binding

Zinc 2

Metal binding

127

Zinc 2

Metal binding

190

Zinc 1

Metal binding

382

Zinc 2

Secondary structure

411

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P77425-1 [UniParc].

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

411

45,694

        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

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References

	« Hide 'large scale' referencesShow '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.

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Cross-references

Sequence databases

U89279 Genomic DNA. Translation: AAB93857.1.
U82664 Genomic DNA. Translation: AAB40268.1.
U00096 Genomic DNA. Translation: AAC73618.1.
AP009048 Genomic DNA. Translation: BAE76294.1.

PIR

C64783.

RefSeq

AP_001164.1.
NP_415049.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z2L	X-ray	2.25	A/B	2-411	[»]
2IMO	X-ray	2.80	A/B	2-411	[»]

ModBase

Search...

Genome annotation databases

GeneID

945150.

GenomeReviews

Gene locus JW0504 in contig AP009048_GR.
Gene locus b0516 in contig U00096_GR.

KEGG

ecj:JW0504.
eco:b0516.

Organism-specific databases

EchoBASE

EB3388.

EcoGene

EG13623. allC.

CMR

Search...

Phylogenomic databases

HOGENOM

P77425.

OMA

P77425. CRHTDAT.

Enzyme and pathway databases

BioCyc

EcoCyc:G6285-MON.
MetaCyc:G6285-MON.

Family and domain databases

InterPro

IPR017591. Allantoate_amidohydrolase.
IPR010158. Amidase_hdtase/Cbmase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]

Pfam

PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]

PIRSF

PIRSF001235. Amidase_carbamoylase. 1 hit.

TIGRFAMs

TIGR03176. AllC. 1 hit.
TIGR01879. hydantase. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

ALLC_ECOLI

Accession

Primary (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:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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