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B8G120

- ALLB_DESHD

UniProt

B8G120 - ALLB_DESHD

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Protein

Allantoinase

Gene
allB, Dhaf_1177
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
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 bindingi61 – 611Zinc 1 By similarity
Metal bindingi63 – 631Zinc 1 By similarity
Metal bindingi148 – 1481Zinc 1; via carbamate group By similarity
Metal bindingi148 – 1481Zinc 2; via carbamate group By similarity
Metal bindingi184 – 1841Zinc 2 By similarity
Metal bindingi240 – 2401Zinc 2 By similarity
Metal bindingi313 – 3131Zinc 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

BioCyciDHAF272564:GCV8-1203-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:Dhaf_1177
OrganismiDesulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Taxonomic identifieri272564 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
ProteomesiUP000007726: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449AllantoinaseUniRule annotationPRO_1000186916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481N6-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

STRINGi272564.Dhaf_1177.

Structurei

3D structure databases

ProteinModelPortaliB8G120.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiRWMSTAP.
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.

B8G120-1 [UniParc]FASTAAdd to Basket

« Hide

MSHYDLILRN GNVVCPDGVR KADIAVSDGK IVLIAEEIPG DAKEIIDAAG    50
KHIFPGITDG HVHFNDPGRT EWETITTGSS ALAAGGGVAY FDMPLNCSPC 100
TLDAVNFNNK LAVAQKDSLV DYGFWGGLTS ANLDKLDELA ECGVIGFKAF 150
ACHSGIDEFP RMDDYTALVG MEKLAKLGLP LMVHCENAEI TKELTELSLA 200
NNRTGVRDYF AARPPITEIE NVSRMITFAE ETGCKLIIAH ISTAKAVELV 250
AQARARGVDV YCETIGHYLY LTGDDVERLG TVAKCSPPIR DGENQLQMWG 300
RLFNDNIAFV SSDHSPCDPK LKNGEFMRVW GGISACQTTL QGLLTHAYHD 350
RKFPLVKIAQ LTAQHVNEIF KIKDKGQIAL GYDADFALVD LDHEFTLQAE 400
DLFYKHKVSP YVGDRFRGSV SQTILRGTTI YKDGKIVSQP IGKHLRPHQ 449
Length:449
Mass (Da):49,300
Last modified:March 3, 2009 - v1
Checksum:i1FBD355BCE3138D3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001336 Genomic DNA. Translation: ACL19235.1.
RefSeqiYP_002457671.1. NC_011830.1.

Genome annotation databases

EnsemblBacteriaiACL19235; ACL19235; Dhaf_1177.
GeneIDi7258147.
KEGGidhd:Dhaf_1177.
PATRICi21660051. VBIDesHaf15223_1226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001336 Genomic DNA. Translation: ACL19235.1 .
RefSeqi YP_002457671.1. NC_011830.1.

3D structure databases

ProteinModelPortali B8G120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272564.Dhaf_1177.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL19235 ; ACL19235 ; Dhaf_1177 .
GeneIDi 7258147.
KEGGi dhd:Dhaf_1177.
PATRICi 21660051. VBIDesHaf15223_1226.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci DHAF272564:GCV8-1203-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. "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive anaerobe capable of dehalogenation and metal reduction."
    Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L., Tiedje J.M.
    BMC Microbiol. 12:21-21(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DCB-2 / DSM 10664.

Entry informationi

Entry nameiALLB_DESHD
AccessioniPrimary (citable) accession number: B8G120
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 38 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

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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