ID   GDAH_RAT                Reviewed;         353 AA.
AC   Q0D2L3; Q5BK25;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Guanidino acid hydrolase, mitochondrial {ECO:0000250|UniProtKB:Q9BSE5};
DE            EC=3.5.3.- {ECO:0000250|UniProtKB:Q9BSE5};
DE   AltName: Full=Arginase, mitochondrial {ECO:0000250|UniProtKB:Q9BSE5};
DE            EC=3.5.3.1 {ECO:0000250|UniProtKB:Q9BSE5};
DE   AltName: Full=Guanidinobutyrase, mitochondrial;
DE            EC=3.5.3.7 {ECO:0000250|UniProtKB:Q9BSE5};
DE   AltName: Full=Guanidinopropionase, mitochondrial;
DE            EC=3.5.3.17 {ECO:0000250|UniProtKB:Q9BSE5};
DE   Flags: Precursor;
GN   Name=Agmat; Synonyms=Gdah {ECO:0000250|UniProtKB:Q9BSE5};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Hydrolyzes linear guanidino acids to form urea and the
CC       corresponding amines. Displays specificity for substrates having a
CC       negatively charged head group and short chains including taurocyamine,
CC       guanidino propanoic and butanoic acids. May protect cells by
CC       detoxifying potentially harmful amounts of guanidino acids. Metabolizes
CC       L-arginine with low efficiency. {ECO:0000250|UniProtKB:Q9BSE5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-guanidinopropanoate + H2O = beta-alanine + urea;
CC         Xref=Rhea:RHEA:16029, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:57593, ChEBI:CHEBI:57966; EC=3.5.3.17;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16030;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-guanidinobutanoate + H2O = 4-aminobutanoate + urea;
CC         Xref=Rhea:RHEA:19501, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:57486, ChEBI:CHEBI:59888; EC=3.5.3.7;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19502;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + taurocyamine = taurine + urea; Xref=Rhea:RHEA:75931,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58064,
CC         ChEBI:CHEBI:507393; EC=3.5.3.17;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75932;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
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:Q9BSE5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20570;
CC         Evidence={ECO:0000250|UniProtKB:Q9BSE5};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={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:Q9BSE5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00742}.
CC   -!- CAUTION: May have little or no activity due to the lack of several
CC       residues essential for manganese binding and catalytic activity.
CC       {ECO:0000305}.
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DR   EMBL; BC091231; AAH91231.1; -; mRNA.
DR   EMBL; BC105628; AAI05629.1; -; mRNA.
DR   RefSeq; NP_001041650.1; NM_001048185.1.
DR   AlphaFoldDB; Q0D2L3; -.
DR   SMR; Q0D2L3; -.
DR   IntAct; Q0D2L3; 1.
DR   STRING; 10116.ENSRNOP00000016646; -.
DR   iPTMnet; Q0D2L3; -.
DR   PhosphoSitePlus; Q0D2L3; -.
DR   PaxDb; 10116-ENSRNOP00000016646; -.
DR   Ensembl; ENSRNOT00000016648.6; ENSRNOP00000016646.3; ENSRNOG00000012315.6.
DR   GeneID; 298607; -.
DR   KEGG; rno:298607; -.
DR   UCSC; RGD:1308424; rat.
DR   AGR; RGD:1308424; -.
DR   CTD; 79814; -.
DR   RGD; 1308424; Agmat.
DR   eggNOG; KOG2964; Eukaryota.
DR   GeneTree; ENSGT00950000183195; -.
DR   HOGENOM; CLU_039478_0_0_1; -.
DR   InParanoid; Q0D2L3; -.
DR   OMA; CIDAGFV; -.
DR   OrthoDB; 161483at2759; -.
DR   PhylomeDB; Q0D2L3; -.
DR   TreeFam; TF328612; -.
DR   Reactome; R-RNO-351143; Agmatine biosynthesis.
DR   UniPathway; UPA00158; UER00270.
DR   PRO; PR:Q0D2L3; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000012315; Expressed in kidney and 16 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR   GO; GO:0004053; F:arginase activity; ISS:UniProtKB.
DR   GO; GO:0047971; F:guanidinobutyrase activity; ISS:UniProtKB.
DR   GO; GO:0047972; F:guanidinopropionase activity; ISS:UniProtKB.
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   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd11592; Agmatinase_PAH; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR005925; Agmatinase-rel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   NCBIfam; TIGR01230; agmatinase; 1.
DR   PANTHER; PTHR11358:SF26; AGMATINASE, MITOCHONDRIAL; 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; PS51409; ARGINASE_2; 1.
DR   Genevisible; Q0D2L3; RN.
PE   2: Evidence at transcript level;
KW   Acetylation; Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..353
FT                   /note="Guanidino acid hydrolase, mitochondrial"
FT                   /id="PRO_0000320073"
FT   REGION          29..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         163
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         188
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   MOD_RES         194
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AS89"
FT   MOD_RES         218
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:A2AS89"
FT   MOD_RES         218
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:A2AS89"
SQ   SEQUENCE   353 AA;  37987 MW;  E59BC1FECE84735A CRC64;
     MLQLLKSSWV RSAGSGVVTW RASAGLFCPG TRQASDTSDT LHHPSPSSES QVQPVRVCSM
     MHLPLQSSPE GLDAAFVGVP LDTGTSNRPG ARFGPRRIRE ESLMLGTVNP STGALPFQSL
     RVADLGNVNV NLYNLQDSCR LIREAYQNIL ATGCIPLTLG GDHTITYPIL QAVAKEHGPV
     GLVHVGAHSN TSDKPLEDKV YHRTPFRRSV DEGLLDSKRV VQIGIRGSSR TLDPYRYSRS
     QGFRVVLAED CWMKSLVPLM AEIRQQMGGV PLYISFAIDA LDPAYAPGTG TPEIAGLTPS
     QALEIIRGCQ GLNVVGCDLV EVSPPYDLSG NTALLAANLL FEMLCALPKV TTV
//