Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O32137 (ALLB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Allantoinase

EC=3.5.2.5
Alternative name(s):
Allantoin-utilizing enzyme
Gene names
Name:allB
Synonyms:pucH, yunH
Ordered Locus Names:BSU32410
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. Ref.2

Catalytic activity

(S)-allantoin + H2O = allantoate. HAMAP-Rule MF_01645

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_01645

Pathway

Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1. HAMAP-Rule MF_01645

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01645

Induction

Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or allantoate are added during limiting-nitrogen conditions. Ref.2

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions By similarity. HAMAP-Rule MF_01645

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Allantoinase HAMAP-Rule MF_01645
PRO_0000165940

Sites

Metal binding601Zinc 1 By similarity
Metal binding621Zinc 1 By similarity
Metal binding1471Zinc 1; via carbamate group By similarity
Metal binding1471Zinc 2; via carbamate group By similarity
Metal binding1831Zinc 2 By similarity
Metal binding2391Zinc 2 By similarity
Metal binding3121Zinc 1 By similarity

Amino acid modifications

Modified residue1471N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O32137 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 48515B6414A5C234

FASTA44648,331
        10         20         30         40         50         60 
MAYDMVIKGA KAVTPDGVIE ADIVVQNGVI AEIGSDIEAS GTEIIQADGK YVFPGVIDCH 

        70         80         90        100        110        120 
VHFNEPGRED WEGFETGSQM MAAGGCTTYF DMPLNCIPST VTAEHLLAKA ELGRQKSAVD 

       130        140        150        160        170        180 
FALWGGLVPG HIEDIRPMAE AGAIGFKAFL SKSGTDEFRS VDERTLLKGM AEIAAAGKIL 

       190        200        210        220        230        240 
ALHAESDAIT SYLQMVLANK GKVDADAYAA SRPEEAEVEA VYRTIQYAKV TGCPVHFVHI 

       250        260        270        280        290        300 
STAKAVRLIR EAKQEGLDVS VETCPHYVLF SHDDLRQRGS VAKCAPPLRS RQSKETLIET 

       310        320        330        340        350        360 
LIAGDIDMVS SDHSPCRPSL KREDNMFLSW GGISGGQFTL LGMLELALEH QIPFETIAEW 

       370        380        390        400        410        420 
TAAAPAKRFG LQKKGRLEAG CDADFVLVSM EPYTVTRESM FAKHKKSIYE GHTFPCSISA 

       430        440 
TYSKGRCVYN DGEKVTEIDG ALVVPS 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
Schultz A.C., Nygaard P., Saxild H.H.
J. Bacteriol. 183:3293-3302(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB15231.1.
PIRC70016.
RefSeqNP_391121.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32137.
SMRO32137. Positions 2-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU32410.

Proteomic databases

PaxDbO32137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15231; CAB15231; BSU32410.
GeneID936662.
KEGGbsu:BSU32410.
PATRIC18978454. VBIBacSub10457_3390.

Organism-specific databases

GenoListBSU32410. [Micado]

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219146.
KOK01466.
OMAAIMLTHV.
OrthoDBEOG6KHFW6.
ProtClustDBPRK06189.

Enzyme and pathway databases

BioCycBSUB:BSU32410-MONOMER.
UniPathwayUPA00395; UER00653.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_01645. Hydantoinase.
InterProIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLB_BACSU
AccessionPrimary (citable) accession number: O32137
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList