ID A0A3P9BYY7_9CICH Unreviewed; 350 AA.
AC A0A3P9BYY7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
DE EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005014841.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005014841.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005014841.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000227,
CC ECO:0000256|RuleBase:RU361159};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361159};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|RuleBase:RU361159};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098,
CC ECO:0000256|RuleBase:RU361159}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR RefSeq; XP_014265276.1; XM_014409790.1.
DR AlphaFoldDB; A0A3P9BYY7; -.
DR STRING; 106582.ENSMZEP00005014841; -.
DR Ensembl; ENSMZET00005015329.1; ENSMZEP00005014841.1; ENSMZEG00005011171.1.
DR GeneID; 101481398; -.
DR KEGG; mze:101481398; -.
DR CTD; 384; -.
DR GeneTree; ENSGT00950000183195; -.
DR OrthoDB; 161483at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000265160; LG19.
DR GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01229; rocF_arginase; 1.
DR PANTHER; PTHR43782; ARGINASE; 1.
DR PANTHER; PTHR43782:SF4; ARGINASE-2, MITOCHONDRIAL; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW ECO:0000256|RuleBase:RU361159};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Manganese {ECO:0000256|RuleBase:RU361159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361159};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Urea cycle {ECO:0000256|ARBA:ARBA00022436, ECO:0000256|RuleBase:RU361159}.
FT REGION 329..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 38362 MW; 90C8FC261F1D4C03 CRC64;
MALRGALSRL SHSSRHFNHT YQQSRAHSVA VLGAPFSKGQ KKRGVEHGPK VIRDAGLMER
LSNFDFSVHD FGDLNFQHLE EDEPYMDVKF PRTVGAANKK LSAAVRNAVS AGHTLLMLGG
DHSLAVGSVS GHAQHSPDLC LIWVDAHADI NTPMTSPSGN LHGQPVAFML KELQDKMPDI
PGFSWTKPFL SSRDLVYIGL RDVDPGEYQF LKSFGIQYFT MRDIDRLGIQ RVMEVTFDHL
LARKQRPIHL SFDIDAFDPS LAPATGTPVN GGLTYREGIY IAEEIHNTGL LSVMDMVEVN
PDLGASPEAV EATATLAVDV IASSLGQTRE GAHTSMDEIP PGKNDTELRL
//
