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InterPro: IPR006680 Amidohydrolase 1
Protein matches
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UniProtKB Matches: 11493 proteins |
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Accession
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IPR006680 Amidohydro_1 |
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Secondary
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IPR002832
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Type
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Domain |
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Signatures
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InterPro Relationships
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Found in
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IPR003764 N-acetylglucosamine-6-phosphate deacetylase
IPR004721 Dihydroorotase homodimeric type
IPR004722 Dihydroorotase multifunctional complex type
IPR005848 Urease, alpha subunit
IPR005920 Imidazolonepropionase
IPR006679 Adenine deaminase
IPR008221 Urease
IPR010229 Peptidase M38, beta-aspartyl dipeptidase
IPR010252 Formiminoglutamate deiminase
IPR011778 D-hydantoinase
IPR012696 Phosphonate metabolism PhnM
IPR014311 Guanine deaminase
IPR017593 Allantoinase
IPR017594 Guanine deaminase, bacterial
IPR017700 Putative selenium metabolism protein SsnA
IPR020043 Amidohydrolase EF0837/AHA3915, putative
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Contains
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IPR002195 Dihydroorotase, conserved site
IPR017950 Urease, alpha subunit, conserved site
IPR017951 Urease, alpha subunit, C-terminal
IPR017952 Urease, alpha subunit, core
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GO Term annotation
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Function
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GO:0016787 hydrolase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This group of enzymes represents a large metal dependent hydrolase superfamily [1]. The family includes adenine deaminase (EC:3.5.4.2) that hydrolyses adenine to form hypoxanthine and ammonia. The adenine deaminase reaction is important for adenine utilization as a purine and also as a nitrogen source [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases (EC:3.5.1.25). These enzymes catalyse the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate This family includes dihydroorotase and urease which belong to MEROPS peptidase family M38 (beta-aspartyl dipeptidase, clan MJ), where they are classified as non-peptidase
homologs.
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Structural links
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SCOP:
b.92.1.1
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b.92.1.10
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b.92.1.11
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b.92.1.3
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b.92.1.4
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b.92.1.5
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b.92.1.7
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b.92.1.8
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c.1.9.10
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c.1.9.13
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c.1.9.14
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c.1.9.16
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c.1.9.17
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c.1.9.2
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c.1.9.4
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c.1.9.6
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c.1.9.9
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Database links
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Pfam Clan: CL0034.11
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Example proteins
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P05990 CAD protein
P32375 Allantoinase
P34480 Putative N-acetylglucosamine-6-phosphate deacetylase
P97427 Dihydropyrimidinase-related protein 1
Q14117 Dihydropyrimidinase
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR011702 |
Glutamine amidotransferase superfamily |
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| IPR002195 |
Dihydroorotase, conserved site |
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| IPR003764 |
N-acetylglucosamine-6-phosphate deacetylase |
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| IPR005479 |
Carbamoyl phosphate synthetase, large subunit, ATP-binding |
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| IPR011761 |
ATP-grasp fold |
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| IPR011059 |
Metal-dependent hydrolase, composite domain |
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| IPR006680 |
Amidohydrolase 1 |
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| IPR000991 |
Glutamine amidotransferase class-I, C-terminal |
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| IPR017593 |
Allantoinase |
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| IPR005481 |
Carbamoyl phosphate synthase, large subunit, N-terminal |
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| IPR005480 |
Carbamoyl phosphate synthetase, large subunit, oligomerisation |
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| IPR013816 |
ATP-grasp fold, subdomain 2 |
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| IPR013817 |
Pre-ATP-grasp fold |
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| IPR002082 |
Aspartate carbamoyltransferase, eukaryotic |
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| IPR005483 |
Carbamoyl phosphate synthase, large subunit |
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| IPR011778 |
D-hydantoinase |
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| IPR017926 |
Glutamine amidotransferase type 1 |
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| IPR016185 |
PreATP-grasp-like fold |
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| IPR006130 |
Aspartate/ornithine carbamoyltransferase |
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| IPR018228 |
Deoxyribonuclease, TatD-related, conserved site |
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| IPR004722 |
Dihydroorotase multifunctional complex type |
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| IPR002474 |
Carbamoyl phosphate synthase, small subunit, N-terminal |
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| IPR006132 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding |
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| IPR006131 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain |
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| IPR011607 |
MGS-like |
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| IPR006275 |
Carbamoyl phosphate synthase, large subunit, glutamine-dependent |
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| IPR006274 |
Carbamoyl phosphate synthase, small subunit |
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| IPR001317 |
Carbamoyl phosphate synthase, GATase domain |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Additional Reading
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Lee M, Maher MJ, Guss JM.
Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibitor 5-fluoroorotate: catalytic activity is reflected by the crystal form.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 154-61
[PubMed: 17329804]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=17329804
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Tyagi R, Kumaran D, Burley SK, Swaminathan S.
X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution.
Proteins 69 2007 652-8
[PubMed: 17640072]
http://dx.doi.org/10.1002/prot.21559
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Jabri E, Carr MB, Hausinger RP, Karplus PA.
The crystal structure of urease from Klebsiella aerogenes.
Science 268 1995 998-1004
[PubMed: 7754395]
http://www.sciencemag.org/cgi/content/abstract/268/5213/998
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Hermann JC, Marti-Arbona R, Fedorov AA, Fedorov E, Almo SC, Shoichet BK, Raushel FM.
Structure-based activity prediction for an enzyme of unknown function.
Nature 448 2007 775-9
[PubMed: 17603473]
http://dx.doi.org/10.1038/nature05981
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Lee M, Maher MJ, Christopherson RI, Guss JM.
Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state.
Biochemistry 46 2007 10538-50
[PubMed: 17711307]
http://dx.doi.org/10.1021/bi701098e
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Gao G, Nara T, Nakajima-Shimada J, Aoki T.
Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi.
J. Mol. Biol. 285 1999 149-61
[PubMed: 9878395]
http://dx.doi.org/10.1006/jmbi.1998.2293
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Tyagi R, Eswaramoorthy S, Burley SK, Raushel FM, Swaminathan S.
A common catalytic mechanism for proteins of the HutI family.
Biochemistry 47 2008 5608-15
[PubMed: 18442260]
http://dx.doi.org/10.1021/bi800180g
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Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL.
As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe.
Curr. Genet. 28 1995 138-49
[PubMed: 8590465]
http://dx.doi.org/10.1007/BF00315780
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InterPro 23.1
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