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Protein

Allantoinase

Gene

allB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.UniRule annotation1 Publication

Catalytic activityi

(S)-allantoin + H2O = allantoate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathway: (S)-allantoin degradation

This protein is involved in step 1 of the subpathway that synthesizes allantoate from (S)-allantoin.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Allantoinase (allB)
This subpathway is part of the pathway (S)-allantoin degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes allantoate from (S)-allantoin, the pathway (S)-allantoin degradation and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Zinc 1UniRule annotation
Metal bindingi62 – 621Zinc 1UniRule annotation
Metal bindingi147 – 1471Zinc 1; via carbamate groupUniRule annotation
Metal bindingi147 – 1471Zinc 2; via carbamate groupUniRule annotation
Metal bindingi183 – 1831Zinc 2UniRule annotation
Metal bindingi239 – 2391Zinc 2UniRule annotation
Metal bindingi312 – 3121Zinc 1UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU32410-MONOMER.
UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
AllantoinaseUniRule annotation (EC:3.5.2.5UniRule annotation)
Alternative name(s):
Allantoin-utilizing enzymeUniRule annotation
Gene namesi
Name:allBUniRule annotation
Synonyms:pucHUniRule annotation, yunH
Ordered Locus Names:BSU32410
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU32410. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446AllantoinasePRO_0000165940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471N6-carboxylysineUniRule annotation

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions.UniRule annotation

Proteomic databases

PaxDbiO32137.

Expressioni

Inductioni

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.1 Publication

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017581.

Structurei

3D structure databases

ProteinModelPortaliO32137.
SMRiO32137. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
InParanoidiO32137.
KOiK01466.
OMAiFMTYDLM.
OrthoDBiEOG6KHFW6.
PhylomeDBiO32137.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

O32137-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYDMVIKGA KAVTPDGVIE ADIVVQNGVI AEIGSDIEAS GTEIIQADGK
60 70 80 90 100
YVFPGVIDCH VHFNEPGRED WEGFETGSQM MAAGGCTTYF DMPLNCIPST
110 120 130 140 150
VTAEHLLAKA ELGRQKSAVD FALWGGLVPG HIEDIRPMAE AGAIGFKAFL
160 170 180 190 200
SKSGTDEFRS VDERTLLKGM AEIAAAGKIL ALHAESDAIT SYLQMVLANK
210 220 230 240 250
GKVDADAYAA SRPEEAEVEA VYRTIQYAKV TGCPVHFVHI STAKAVRLIR
260 270 280 290 300
EAKQEGLDVS VETCPHYVLF SHDDLRQRGS VAKCAPPLRS RQSKETLIET
310 320 330 340 350
LIAGDIDMVS SDHSPCRPSL KREDNMFLSW GGISGGQFTL LGMLELALEH
360 370 380 390 400
QIPFETIAEW TAAAPAKRFG LQKKGRLEAG CDADFVLVSM EPYTVTRESM
410 420 430 440
FAKHKKSIYE GHTFPCSISA TYSKGRCVYN DGEKVTEIDG ALVVPS
Length:446
Mass (Da):48,331
Last modified:January 1, 1998 - v1
Checksum:i48515B6414A5C234
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15231.1.
PIRiC70016.
RefSeqiNP_391121.1. NC_000964.3.
WP_003243112.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15231; CAB15231; BSU32410.
GeneIDi936662.
KEGGibsu:BSU32410.
PATRICi18978454. VBIBacSub10457_3390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15231.1.
PIRiC70016.
RefSeqiNP_391121.1. NC_000964.3.
WP_003243112.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO32137.
SMRiO32137. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017581.

Proteomic databases

PaxDbiO32137.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15231; CAB15231; BSU32410.
GeneIDi936662.
KEGGibsu:BSU32410.
PATRICi18978454. VBIBacSub10457_3390.

Organism-specific databases

GenoListiBSU32410. [Micado]

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
InParanoidiO32137.
KOiK01466.
OMAiFMTYDLM.
OrthoDBiEOG6KHFW6.
PhylomeDBiO32137.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.
BioCyciBSUB:BSU32410-MONOMER.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiALLB_BACSU
AccessioniPrimary (citable) accession number: O32137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.