SPEB_CHICK
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 03-AUG-2022, entry version 126.
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;
CC Evidence={ECO:0000255|PROSITE-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.ENSGALP00000022199; -.
DR PaxDb; Q90XD2; -.
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 OrthoDB; 921352at2759; -.
DR PhylomeDB; Q90XD2; -.
DR TreeFam; TF328612; -.
DR UniPathway; UPA00534; UER00287.
DR PRO; PR:Q90XD2; -.
DR Proteomes; UP000000539; Unplaced.
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 InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 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
