ARGI_EMENI
ID ARGI_EMENI Reviewed; 324 AA.
AC Q12611; C8VJ82; Q5B979;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=agaA; ORFNames=AN2901;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10547040;
RA Borsuk P., Dzikowska A., Empel J., Grzelak A., Grzeskowiak R.,
RA Weglenski P.;
RT "Structure of the arginase coding gene and its transcript in Aspergillus
RT nidulans.";
RL Acta Biochim. Pol. 46:391-403(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000250|UniProtKB:P05089};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; U62482; AAB05775.1; -; Genomic_DNA.
DR EMBL; AACD01000051; EAA63472.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83783.1; -; Genomic_DNA.
DR RefSeq; XP_660505.1; XM_655413.1.
DR AlphaFoldDB; Q12611; -.
DR SMR; Q12611; -.
DR STRING; 162425.CADANIAP00010188; -.
DR EnsemblFungi; CBF83783; CBF83783; ANIA_02901.
DR EnsemblFungi; EAA63472; EAA63472; AN2901.2.
DR GeneID; 2873985; -.
DR KEGG; ani:AN2901.2; -.
DR VEuPathDB; FungiDB:AN2901; -.
DR eggNOG; KOG2965; Eukaryota.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q12611; -.
DR OMA; IATCFGQ; -.
DR OrthoDB; 1179130at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004053; F:arginase activity; IDA:AspGD.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..324
FT /note="Arginase"
FT /id="PRO_0000173708"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 145..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT CONFLICT 35
FT /note="E -> V (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="I -> V (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="A -> G (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="S -> R (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="Missing (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> V (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="R -> C (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="E -> V (in Ref. 1; AAB05775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35479 MW; 5767BEB9D7987A16 CRC64;
MTSPSTIKQR FLSKPNQLGV VAVGFNGGQC KLGVEAAPMA LVEAGLLDQL RDDLDYEIHY
DNTVHYYEKE IPAEDPDHRG MKKPRAVSAV TETLSSQVYE HSKEGKFTLT LGGDHSIAIG
SISGIAKATR ERLGREIGVI WVDAHADINI PEMSPSGNIH GMPMAFLTRL ATEEKKDIFG
WLQEEHKVNL RKLVYIGLRD VDRGEKKLLR EHGIKAFSMH DVDRHGIGRV VEMALAHIGN
DTPIHLSFDV DALDPQWAPS TGTPVRGGLT LREGDFICEC VHETGNLISM DLVEVNPSLE
AVGASDTIRT GCSLVRSALG DTLL
