Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O32137

- ALLB_BACSU

UniProt

O32137 - ALLB_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Allantoinase

Gene

allB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

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

Pathwayi

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

  1. allantoinase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. allantoin catabolic process Source: UniProtKB-HAMAP
  2. purine nucleobase metabolic process Source: UniProtKB-KW
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: 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.BSU32410.

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.
OMAiRWMSTAP.
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.

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 .
PIRi C70016.
RefSeqi NP_391121.1. NC_000964.3.

3D structure databases

ProteinModelPortali O32137.
SMRi O32137. Positions 2-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU32410.

Proteomic databases

PaxDbi O32137.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15231 ; CAB15231 ; BSU32410 .
GeneIDi 936662.
KEGGi bsu:BSU32410.
PATRICi 18978454. VBIBacSub10457_3390.

Organism-specific databases

GenoListi BSU32410. [Micado ]

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219146.
InParanoidi O32137.
KOi K01466.
OMAi RWMSTAP.
OrthoDBi EOG6KHFW6.
PhylomeDBi O32137.

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci BSUB:BSU32410-MONOMER.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01645. Hydantoinase.
InterProi IPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 108 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