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Reviewed, UniProtKB/Swiss-Prot O32137 (ALLB_BACSU)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 + H(2)O = allantoate. HAMAP MF_01645

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

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

Subunit structure

Homotetramer By similarity.

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.

Sequence similarities

Belongs to the DHOase family. Allantoinase subfamily.

Ontologies

Keywords

   Biological processPurine metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processallantoin catabolic process

Inferred from electronic annotation. Source: HAMAP

purine base metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionallantoinase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Allantoinase HAMAP 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
O32137-1 [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: 9384377] [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: 11344136] [Abstract]
Cited for: FUNCTION, INDUCTION.
Strain: 168.

Cross-references

Sequence databases

Z99120 Genomic DNA. Translation: CAB15231.1.
PIRC70016.
RefSeqNP_391121.1.

3D structure databases

HSSPHSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBaseSearch...

Genome annotation databases

GeneID936662.
GenomeReviewsGene locus BSU32410 in contig AL009126_GR.
KEGGbsu:BSU32410.
NMPDRfig|224308.1.peg.3247.

Organism-specific databases

SubtiListBG13982. pucH. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO32137.

Enzyme and pathway databases

BioCycBSUB224308:BSU3238-MON.

Family and domain databases

HAMAPMF_01645.
[Tree]
InterProIPR017593. Allantoinase.
IPR006680. Amidohydro_1.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
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: November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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