Skip Header

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

Q9KAH8

- ALLB_BACHD

UniProt

Q9KAH8 - ALLB_BACHD

(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 halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - 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 Zn(2+) ions per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Zinc 1UniRule annotation
Metal bindingi65 – 651Zinc 1UniRule annotation
Metal bindingi150 – 1501Zinc 1; via carbamate groupUniRule annotation
Metal bindingi150 – 1501Zinc 2; via carbamate groupUniRule annotation
Metal bindingi186 – 1861Zinc 2UniRule annotation
Metal bindingi242 – 2421Zinc 2UniRule annotation
Metal bindingi315 – 3151Zinc 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

BioCyciBHAL272558:GJC5-2393-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
Ordered Locus Names:BH2309
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438AllantoinasePRO_0000317670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501N6-carboxylysineUniRule annotation

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

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi19 – 279Combined sources
Beta strandi30 – 367Combined sources
Beta strandi47 – 493Combined sources
Beta strandi54 – 574Combined sources
Beta strandi59 – 646Combined sources
Turni68 – 703Combined sources
Helixi72 – 743Combined sources
Helixi78 – 858Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 1016Combined sources
Helixi106 – 1138Combined sources
Helixi115 – 1195Combined sources
Beta strandi121 – 1299Combined sources
Helixi135 – 1373Combined sources
Helixi138 – 1436Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi157 – 1615Combined sources
Helixi166 – 17914Combined sources
Beta strandi183 – 1864Combined sources
Helixi190 – 20213Combined sources
Helixi208 – 2147Combined sources
Helixi217 – 23418Combined sources
Beta strandi238 – 2403Combined sources
Helixi246 – 25712Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 2725Combined sources
Helixi275 – 2817Combined sources
Helixi294 – 30613Combined sources
Helixi321 – 3244Combined sources
Turni329 – 3313Combined sources
Turni339 – 3413Combined sources
Helixi342 – 3498Combined sources
Turni350 – 3545Combined sources
Helixi358 – 3658Combined sources
Helixi367 – 3737Combined sources
Turni376 – 3783Combined sources
Beta strandi390 – 40011Combined sources
Helixi403 – 4053Combined sources
Beta strandi408 – 4103Combined sources
Turni414 – 4174Combined sources
Beta strandi419 – 42911Combined sources
Beta strandi432 – 4365Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9KAH8.

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0044.
HOGENOMiHOG000219146.
KOiK01466.
OMAiCSPWEGH.
OrthoDBiEOG6KHFW6.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
HAMAPiMF_01645. Hydantoinase.
InterProiIPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
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.
RefSeqiNP_243175.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB06028; BAB06028; BAB06028.
GeneIDi892154.
KEGGibha:BH2309.
PATRICi18941796. VBIBacHal18977_2411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06028.1 .
PIRi E83938.
RefSeqi NP_243175.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HM7 X-ray 2.60 A/B/C/D/E/F 2-438 [» ]
ProteinModelPortali Q9KAH8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH2309.

Protocols and materials databases

DNASUi 892154.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB06028 ; BAB06028 ; BAB06028 .
GeneIDi 892154.
KEGGi bha:BH2309.
PATRICi 18941796. VBIBacHal18977_2411.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00395 ; UER00653 .
BioCyci BHAL272558:GJC5-2393-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9KAH8.

Family and domain databases

Gene3Di 2.30.40.10. 1 hit.
HAMAPi MF_01645. Hydantoinase.
InterProi IPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

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 26, 2014
This is version 88 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

External Data

Dasty 3