ID   ARGI2_SCHPO             Reviewed;         323 AA.
AC   Q10066;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Arginase;
DE            EC=3.5.3.1;
GN   Name=aru1; ORFNames=SPAC3H1.07;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RA   Ocampos M.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY: L-arginine + H(2)O = L-ornithine + urea.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea
CC       from L-arginine: step 1/1.
CC   -!- SUBUNIT: Homotrimer (By similarity).
CC   -!- SIMILARITY: Belongs to the arginase family.
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DR   EMBL; U24279; AAA65456.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA92260.1; -; Genomic_DNA.
DR   PIR; T38739; T38739.
DR   PIR; T52537; T52537.
DR   RefSeq; NP_593549.1; -.
DR   HSSP; P78540; 1PQ3.
DR   GeneID; 2543377; -.
DR   KEGG; spo:SPAC3H1.07; -.
DR   NMPDR; fig|4896.1.peg.3519; -.
DR   GeneDB_Spombe; SPAC3H1.07; -.
DR   OMA; Q10066; QIVKNPR.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-001226-MON; -.
DR   BRENDA; 3.5.3.1; 653.
DR   ArrayExpress; Q10066; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0004053; F:arginase activity; IEA:EC.
DR   GO; GO:0030145; F:manganese 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-KW.
DR   InterPro; IPR005924; Arginase.
DR   InterPro; IPR014033; Arginase_sub.
DR   InterPro; IPR006035; Ureohydrolase.
DR   Gene3D; G3DSA:3.40.800.10; Ureohydrolase; 1.
DR   PANTHER; PTHR11358:SF2; Arginase_sub; 1.
DR   PANTHER; PTHR11358; Ureohydrolase; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Arginine metabolism; Complete proteome; Hydrolase; Manganese;
KW   Metal-binding; Urea cycle.
FT   CHAIN         1    323       Arginase.
FT                                /FTId=PRO_0000173710.
FT   REGION      144    148       Substrate binding (By similarity).
FT   REGION      155    157       Substrate binding (By similarity).
FT   METAL       119    119       Manganese 1 (By similarity).
FT   METAL       142    142       Manganese 1 (By similarity).
FT   METAL       142    142       Manganese 2 (By similarity).
FT   METAL       144    144       Manganese 2 (By similarity).
FT   METAL       146    146       Manganese 1 (By similarity).
FT   METAL       247    247       Manganese 1 (By similarity).
FT   METAL       247    247       Manganese 2 (By similarity).
FT   METAL       249    249       Manganese 2 (By similarity).
FT   BINDING     198    198       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
FT   CONFLICT    278    278       A -> R (in Ref. 1; AAA65456).
FT   CONFLICT    293    294       Missing (in Ref. 1; AAA65456).
SQ   SEQUENCE   323 AA;  35704 MW;  1E10876E0E969D66 CRC64;
     MSPHKISDNH RHLMLSRFMM GNGVSIINMP FSGGQPKDGA ELAPEMVEKA GLVDDLEHLG
     YDVKLIQNPE FKSRPSKEGP NQALMKNPLY VSNVTRQVRD AVQRELEQQR VVVNIGGDHS
     LAIGTVEGVQ AVYDDACVLW IDAHADINTP ESSPSKNLHG CPLSFSLGYA EPLPEEFAWT
     KRVIEERRLA FIGLRDLDPM ERAFLRERNI AAYTMHHVDK YGIGRVVEMA MEHINPGKRR
     PVHLSFDVDA CDPIVAPATG TRVPGGLTFR EAMYICEAVA ESGTLVAVDV MEVNPLLGNE
     EEAKTTVDLA RSIVRTSLGQ TLL
//