Q12611 (ARGI_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginase
EC=3.5.3.1

Gene names

Name:	agaA
ORF Names:	AN2901

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subunit structure	Homotrimer By similarity.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	arginase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 324	324	Arginase		PRO_0000173708
Regions
	Region	145 – 149	5	Substrate binding By similarity
	Region	156 – 158	3	Substrate binding By similarity
Sites
	Metal binding	115	1	Manganese 1 By similarity
	Metal binding	143	1	Manganese 1 By similarity
	Metal binding	143	1	Manganese 2 By similarity
	Metal binding	145	1	Manganese 2 By similarity
	Metal binding	147	1	Manganese 1 By similarity
	Metal binding	249	1	Manganese 1 By similarity
	Metal binding	249	1	Manganese 2 By similarity
	Metal binding	251	1	Manganese 2 By similarity
	Binding site	202	1	Substrate By similarity
	Binding site	294	1	Substrate By similarity
Experimental info
	Sequence conflict	35	1	E → V in AAB05775. Ref.1
	Sequence conflict	71	1	I → V in AAB05775. Ref.1
	Sequence conflict	86	1	A → G in AAB05775. Ref.1
	Sequence conflict	95	1	S → R in AAB05775. Ref.1
	Sequence conflict	132	1	Missing in AAB05775. Ref.1
	Sequence conflict	258	1	A → V in AAB05775. Ref.1
	Sequence conflict	272	1	R → C in AAB05775. Ref.1
	Sequence conflict	300	1	E → V in AAB05775. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q12611 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 5767BEB9D7987A16	FASTA	324	35,479
	10 20 30 40 50 60 MTSPSTIKQR FLSKPNQLGV VAVGFNGGQC KLGVEAAPMA LVEAGLLDQL RDDLDYEIHY 70 80 90 100 110 120 DNTVHYYEKE IPAEDPDHRG MKKPRAVSAV TETLSSQVYE HSKEGKFTLT LGGDHSIAIG 130 140 150 160 170 180 SISGIAKATR ERLGREIGVI WVDAHADINI PEMSPSGNIH GMPMAFLTRL ATEEKKDIFG 190 200 210 220 230 240 WLQEEHKVNL RKLVYIGLRD VDRGEKKLLR EHGIKAFSMH DVDRHGIGRV VEMALAHIGN 250 260 270 280 290 300 DTPIHLSFDV DALDPQWAPS TGTPVRGGLT LREGDFICEC VHETGNLISM DLVEVNPSLE 310 320 AVGASDTIRT GCSLVRSALG DTLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the arginase coding gene and its transcript in Aspergillus nidulans." Borsuk P., Dzikowska A., Empel J., Grzelak A., Grzeskowiak R., Weglenski P. Acta Biochim. Pol. 46:391-403(1999) [PubMed: 10547040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62482 Genomic DNA. Translation: AAB05775.1. AACD01000051 Genomic DNA. Translation: EAA63472.1. BN001306 Genomic DNA. Translation: CBF83783.1.
RefSeq	XP_660505.1. XM_655413.1.
3D structure databases
ProteinModelPortal	Q12611.
ModBase	Search...
Protein-protein interaction databases
STRING	Q12611.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00010188; CADANIAP00010188; CADANIAG00010188.
GeneID	2873985.
KEGG	ani:AN2901.2.
Phylogenomic databases
OMA	HADINIP.
OrthoDB	EOG432471.
PhylomeDB	Q12611.
Family and domain databases
InterPro	IPR014033. Arginase_subgr. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KO	K01476.
PANTHER	PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01229. RocF_arginase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGI_EMENI

Accession

Primary (citable) accession number: Q12611
Secondary accession number(s): C8VJ82, Q5B979

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 2007
Last modified:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program