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Q9RV76

- ALLB_DEIRA

UniProt

Q9RV76 - ALLB_DEIRA

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Protein
Allantoinase
Gene
allB, DR_1153
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit By similarity.UniRule annotation

Pathwayi

Sites

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

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

BioCyciDRAD243230:GH46-1180-MONOMER.
UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Allantoinase (EC:3.5.2.5)
Alternative name(s):
Allantoin-utilizing enzyme
Gene namesi
Name:allB
Ordered Locus Names:DR_1153
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448AllantoinaseUniRule annotation
PRO_0000165941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471N6-carboxylysine By similarity

Post-translational modificationi

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

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243230.DR_1153.

Structurei

3D structure databases

ProteinModelPortaliQ9RV76.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiCSPWEGH.
OrthoDBiEOG6KHFW6.

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.

Q9RV76-1 [UniParc]FASTAAdd to Basket

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MSLDLLLRGA VLVTPEGERR ADLGIVGGQI AELTDEIATP AAQTLDVSGL    50
HVFPGVLDDH VHLNEPGRTH WEGFETGTQA LAAGGATSFL DMPLNSSPPV 100
LTRERFEDKA RLGEEKSLID FGLWGGLTPL NLDQLDDLAE CGVIGLKAFM 150
SHSGLDEFPA ADDLTLYEGM RTAKRHGLVV ATHAESNEFT RRLTETARAQ 200
GKSGVRDYLE SRPVVTELEA VQRALLFAQD TGAALHLVHV SSGAAVALAY 250
EGKQKGIDVT IETCPHYLHF TGEDVERVGA ALKCAPPLRD PAVQEELWRE 300
LLAGHIDTVG SDHSPAPPDM KTSEDFFSLW GGISGAQSTL NVMLEDGYAQ 350
RGLPLEIIAA LLALNPAQRF GLPQKGRLAV GADADFALVA LGEKFTLDTL 400
YDRWQQNPYR GQSFQGRVHA TYLRGQPVYQ NGEFTGTPRG RLLRPRSL 448
Length:448
Mass (Da):48,559
Last modified:May 1, 2000 - v1
Checksum:i3215965D0613AF86
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF10727.1.
PIRiE75429.
RefSeqiNP_294877.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10727; AAF10727; DR_1153.
GeneIDi1798402.
KEGGidra:DR_1153.
PATRICi21629898. VBIDeiRad64572_1350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF10727.1 .
PIRi E75429.
RefSeqi NP_294877.1. NC_001263.1.

3D structure databases

ProteinModelPortali Q9RV76.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_1153.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF10727 ; AAF10727 ; DR_1153 .
GeneIDi 1798402.
KEGGi dra:DR_1153.
PATRICi 21629898. VBIDeiRad64572_1350.

Phylogenomic databases

eggNOGi COG0044.
HOGENOMi HOG000219146.
KOi K01466.
OMAi CSPWEGH.
OrthoDBi EOG6KHFW6.

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci DRAD243230:GH46-1180-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiALLB_DEIRA
AccessioniPrimary (citable) accession number: Q9RV76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 103 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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