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Protein

Allantoinase

Gene

allB

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

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

Pathwayi: (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)DescriptionActionsGraphical viewLength
Metal bindingi63Zinc 1UniRule annotation1
Metal bindingi65Zinc 1UniRule annotation1
Metal bindingi150Zinc 1; via carbamate groupUniRule annotation1
Metal bindingi150Zinc 2; via carbamate groupUniRule annotation1
Metal bindingi186Zinc 2UniRule annotation1
Metal bindingi242Zinc 2UniRule annotation1
Metal bindingi315Zinc 1UniRule annotation1

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

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
Ordered Locus Names:BH2309
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003176701 – 438AllantoinaseAdd BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei150N6-carboxylysineUniRule annotation1

Post-translational modificationi

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

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272558.BH2309.

Structurei

Secondary structure

1438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Beta strandi19 – 27Combined sources9
Beta strandi30 – 36Combined sources7
Beta strandi47 – 49Combined sources3
Beta strandi54 – 57Combined sources4
Beta strandi59 – 64Combined sources6
Turni68 – 70Combined sources3
Helixi72 – 74Combined sources3
Helixi78 – 85Combined sources8
Turni86 – 88Combined sources3
Beta strandi89 – 94Combined sources6
Beta strandi96 – 101Combined sources6
Helixi106 – 113Combined sources8
Helixi115 – 119Combined sources5
Beta strandi121 – 129Combined sources9
Helixi135 – 137Combined sources3
Helixi138 – 143Combined sources6
Beta strandi147 – 155Combined sources9
Beta strandi157 – 161Combined sources5
Helixi166 – 179Combined sources14
Beta strandi183 – 186Combined sources4
Helixi190 – 202Combined sources13
Helixi208 – 214Combined sources7
Helixi217 – 234Combined sources18
Beta strandi238 – 240Combined sources3
Helixi246 – 257Combined sources12
Beta strandi262 – 266Combined sources5
Helixi268 – 272Combined sources5
Helixi275 – 281Combined sources7
Helixi294 – 306Combined sources13
Helixi321 – 324Combined sources4
Turni329 – 331Combined sources3
Turni339 – 341Combined sources3
Helixi342 – 349Combined sources8
Turni350 – 354Combined sources5
Helixi358 – 365Combined sources8
Helixi367 – 373Combined sources7
Turni376 – 378Combined sources3
Beta strandi390 – 400Combined sources11
Helixi403 – 405Combined sources3
Beta strandi408 – 410Combined sources3
Turni414 – 417Combined sources4
Beta strandi419 – 429Combined sources11
Beta strandi432 – 436Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HM7X-ray2.60A/B/C/D/E/F2-438[»]
ProteinModelPortaliQ9KAH8.
SMRiQ9KAH8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KAH8.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107RNN. Bacteria.
COG0044. LUCA.
HOGENOMiHOG000219146.
KOiK01466.
OMAiIEAHAHI.
OrthoDBiPOG091H02CH.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase. 1 hit.
InterProiIPR017593. Allantoinase.
IPR006680. Amidohydro-rel.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9KAH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRFDLIIRS STVVTETTTY RADVAIRNGI VSAITEPGSI SSDDGPAIDG
60 70 80 90 100
TGLHLFPGMV DVHVHFNEPG RTEWEGFASG SKSLAAGGVT TYFDMPLNSN
110 120 130 140 150
PPTITREELD KKRQLANEKS LVDYRFWGGL VPGNIDHLQD LHDGGVIGFK
160 170 180 190 200
AFMSECGTDD FQFSHDETLL KGMKKIAALG SILAVHAESN EMVNALTTIA
210 220 230 240 250
IEEQRLTVKD YSEARPIVSE LEAVERILRF AQLTCCPIHI CHVSSRKVLK
260 270 280 290 300
RIKQAKGEGV NVSVETCPHY LLFSLDEFAE IGYLAKCAPP LRERQEVEDL
310 320 330 340 350
WDGLMAGEID LISSDHSPSL PQMKTGKTIF EVWGGIAGCQ NTLAVMLTEG
360 370 380 390 400
YHKRKMPLTQ IVQLLSTEPA KRFGLYPQKG TIQVGAEASF TLIDLNESYT
410 420 430
LNASDLYYRH PISPYVGQRF RGKVKHTICQ GKHVYQDH
Length:438
Mass (Da):48,542
Last modified:October 1, 2000 - v1
Checksum:i47A24DD790AF947F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06028.1.
PIRiE83938.
RefSeqiWP_010898465.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB06028; BAB06028; BAB06028.
KEGGibha:BH2309.
PATRICi18941796. VBIBacHal18977_2411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06028.1.
PIRiE83938.
RefSeqiWP_010898465.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HM7X-ray2.60A/B/C/D/E/F2-438[»]
ProteinModelPortaliQ9KAH8.
SMRiQ9KAH8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH2309.

Protocols and materials databases

DNASUi892154.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB06028; BAB06028; BAB06028.
KEGGibha:BH2309.
PATRICi18941796. VBIBacHal18977_2411.

Phylogenomic databases

eggNOGiENOG4107RNN. Bacteria.
COG0044. LUCA.
HOGENOMiHOG000219146.
KOiK01466.
OMAiIEAHAHI.
OrthoDBiPOG091H02CH.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.

Miscellaneous databases

EvolutionaryTraceiQ9KAH8.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase. 1 hit.
InterProiIPR017593. Allantoinase.
IPR006680. Amidohydro-rel.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALLB_BACHD
AccessioniPrimary (citable) accession number: Q9KAH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 99 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.