ID   SPEB3_SCHPO             Reviewed;         408 AA.
AC   Q9C0Y9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Putative agmatinase 3;
DE            EC=3.5.3.11 {ECO:0000250|UniProtKB:Q9BSE5};
DE   AltName: Full=Agmatine ureohydrolase 3;
DE            Short=AUH 3;
DE   Flags: Precursor;
GN   ORFNames=SPAPB24D3.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC         ChEBI:CHEBI:326268; EC=3.5.3.11;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00742};
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742}.
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DR   EMBL; CU329670; CAC36899.2; -; Genomic_DNA.
DR   RefSeq; NP_593990.2; NM_001019416.2.
DR   AlphaFoldDB; Q9C0Y9; -.
DR   SMR; Q9C0Y9; -.
DR   BioGRID; 279984; 6.
DR   STRING; 284812.Q9C0Y9; -.
DR   iPTMnet; Q9C0Y9; -.
DR   PaxDb; 4896-SPAPB24D3-03-1; -.
DR   EnsemblFungi; SPAPB24D3.03.1; SPAPB24D3.03.1:pep; SPAPB24D3.03.
DR   GeneID; 2543569; -.
DR   KEGG; spo:SPAPB24D3.03; -.
DR   PomBase; SPAPB24D3.03; -.
DR   VEuPathDB; FungiDB:SPAPB24D3.03; -.
DR   eggNOG; KOG2964; Eukaryota.
DR   HOGENOM; CLU_039478_1_1_1; -.
DR   InParanoid; Q9C0Y9; -.
DR   OMA; YHIPNAM; -.
DR   PRO; PR:Q9C0Y9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
DR   CDD; cd11592; Agmatinase_PAH; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358:SF30; AGMATINASE 1-RELATED; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 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   Hydrolase; Manganese; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..408
FT                   /note="Putative agmatinase 3"
FT                   /id="PRO_0000311760"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         224
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         319
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         319
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         321
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
SQ   SEQUENCE   408 AA;  45085 MW;  3BB0F4614304C536 CRC64;
     MKSVEWFTWG VFLLLSGFGE AGRMGLGFQE KNPVFVKEKQ SPFYAVPSNY EEVEFSSIVE
     PMYSGIATFG RLENVECLSK RSEDFDIAFI GMPFDTGTSY RPGARFGPSS LREGSRRINT
     KYGAVNVPLE INPFKSWAKL VDCGDIPVTT YDILKAMDQL ESAYFQLIAR KPSSFTDHDG
     FAKNDTVLPR VLSLGGDHTI VLPILRALHR VYGQPISVIH FDSHLDTWAP GLIGDGDEAD
     GINHGSYFYF ASQEGIMSKD ANIHAGIRTP ISSFSDYDDD VDCGFKIIEA REIDDLGIDG
     IVKKIRDRVG DNLVYLSIDI DVLDPAFAPA TGTPETGGWS SREMRAILRG LQGLKFVGAD
     LVEVAPAYDV AEITSLAGAQ LLFDIVSMMV KYPLVKEADL SRYMPIHK
//