ID   SPEB_CHICK              Reviewed;         340 AA.
AC   Q90XD2;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Agmatinase, mitochondrial;
DE            EC=3.5.3.11 {ECO:0000250|UniProtKB:Q9BSE5};
DE   AltName: Full=Agmatine ureohydrolase;
DE            Short=AUH;
DE   Flags: Precursor;
GN   Name=AGMAT;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Morris S.M. Jr., Kepka-Lenhart D.;
RT   "Identification of chicken agmatinase.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; putrescine from agmatine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q9BSE5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00742}.
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DR   EMBL; AF401291; AAK97629.1; -; mRNA.
DR   RefSeq; NP_989474.1; NM_204143.2.
DR   AlphaFoldDB; Q90XD2; -.
DR   SMR; Q90XD2; -.
DR   STRING; 9031.ENSGALP00000049981; -.
DR   PaxDb; 9031-ENSGALP00000022199; -.
DR   GeneID; 373942; -.
DR   KEGG; gga:373942; -.
DR   CTD; 79814; -.
DR   VEuPathDB; HostDB:geneid_373942; -.
DR   eggNOG; KOG2964; Eukaryota.
DR   HOGENOM; CLU_039478_0_0_1; -.
DR   InParanoid; Q90XD2; -.
DR   PhylomeDB; Q90XD2; -.
DR   TreeFam; TF328612; -.
DR   UniPathway; UPA00534; UER00287.
DR   PRO; PR:Q90XD2; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR020855; Ureohydrolase_Mn_BS.
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; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Mitochondrion;
KW   Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..340
FT                   /note="Agmatinase, mitochondrial"
FT                   /id="PRO_0000002090"
FT   BINDING         150
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         177
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         264
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         264
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         266
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
SQ   SEQUENCE   340 AA;  36488 MW;  305E113C32F75F89 CRC64;
     MICLLRTARL SARLLFASAA APCRRASRFN VPPSAEFVAR PVGVCSMLRL PVQTSAEGLD
     AAFVGVPLDT GTSNRPGARF GPQQIRAESV MVRRYNASTG AAPFDSLLVA DVGDVNVNLY
     NLPDSCRRIR ESYQKIVASG CVPLTLGGDH SITYPILQAV AEKHGPVGLV HVDAHTDTSD
     MALGEKIYHG TPFRRCVDEG LLDCSRVVQI GIRGSSYAPN PYKYCWDQGF RVVPAEECWM
     KSLVPLMGEV RQQMGDGPVY ISFDIDGLDP AYAPGTGTPE IAGLTPMQAL EIIRGCKGLN
     IVGCDLVEVA PIYDVSGNTA LLGANLLFEM LCVLPGVKTM
//