Skip Header

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

Allantoinase, mitochondrial

Gene

ALN

Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-allantoin + H2O = allantoate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi76 – 761Zinc 1By similarity
Metal bindingi78 – 781Zinc 1By similarity
Metal bindingi163 – 1631Zinc 1; via carbamate groupBy similarity
Metal bindingi163 – 1631Zinc 2; via carbamate groupBy similarity
Metal bindingi199 – 1991Zinc 2By similarity
Metal bindingi251 – 2511Zinc 2By similarity
Metal bindingi324 – 3241Zinc 1By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. allantoin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Allantoinase, mitochondrial (EC:3.5.2.5)
Gene namesi
Name:ALN
OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifieri8400 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 484Allantoinase, mitochondrialPRO_0000007371
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei163 – 1631N6-carboxylysineBy similarity

Post-translational modificationi

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

Expressioni

Tissue specificityi

Liver and kidney.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP40757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Allantoinase subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG004211.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
InterProiIPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKSKPGIM NITPGSKISV IRSKRVIQAN TISSCDIIIS DGKISSVLAW
60 70 80 90 100
GKHVTSGAKL LDVGDLVVMA GIIDPHVHVN EPGRTDWEGY RTATLAAAAG
110 120 130 140 150
GITAIVDMPL NSLPPTTSVT NFHTKLQAAK RQCYVDVAFW GGVIPDNQVE
160 170 180 190 200
LIPMLQAGVA GFKCFLINSG VPEFPHVSVT DLHTAMSELQ GTNSVLLFHA
210 220 230 240 250
ELEIAKPAPE IGDSTLYQTF LDSRPDDMEI AAVQLVADLC QQYKVRCHIV
260 270 280 290 300
HLSSAQSLTI IRKAKEAGAP LTVETTHHYL SLSSEHIPPG ATYFKCCPPV
310 320 330 340 350
RGHRNKEALW NALLQGHIDM VVSDHSPCTP DLKLLKEGDY MKAWGGISSL
360 370 380 390 400
QFGLPLFWTS ARTRGFSLTD VSQLLSSNTA KLCGLGIVKE PLKWVMMLIW
410 420 430 440 450
SSGILTKSFR CKKMIFITRI SSPHIWDSFF KEKSWLLLFE GLLFISKGSM
460 470 480
LPNQLENLFL YTLWSLVKPV HPVHPIIRKN LPHI
Length:484
Mass (Da):53,257
Last modified:February 1, 1995 - v1
Checksum:iA2DC377B850DC402
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03471 mRNA. Translation: AAA19116.1.
PIRiA53595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03471 mRNA. Translation: AAA19116.1.
PIRiA53595.

3D structure databases

ProteinModelPortaliP40757.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004211.

Enzyme and pathway databases

UniPathwayiUPA00395; UER00653.

Family and domain databases

Gene3Di2.30.40.10. 1 hit.
InterProiIPR017593. Allantoinase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 1 hit.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amphibian allantoinase. Molecular cloning, tissue distribution, and functional expression."
    Hayashi S., Jain S., Chu R., Alvares K., Xu B., Erfurth F., Usuda N., Rao M.S., Reddy S.K., Noguchi T., Reddy J.K., Yeldandi A.Y.
    J. Biol. Chem. 269:12269-12276(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 365-381.
    Tissue: Liver.

Entry informationi

Entry nameiALN_LITCT
AccessioniPrimary (citable) accession number: P40757
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.