SPEB_RAT
ID SPEB_RAT Reviewed; 353 AA.
AC Q0D2L3; Q5BK25;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 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 -!- 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}.
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; Q0D2L3; -.
DR PRIDE; Q0D2L3; -.
DR Ensembl; ENSRNOT00000016648; ENSRNOP00000016646; ENSRNOG00000012315.
DR GeneID; 298607; -.
DR KEGG; rno:298607; -.
DR UCSC; RGD:1308424; rat.
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; 921352at2759; -.
DR PhylomeDB; Q0D2L3; -.
DR TreeFam; TF328612; -.
DR Reactome; R-RNO-351143; Agmatine biosynthesis.
DR UniPathway; UPA00534; UER00287.
DR PRO; PR:Q0D2L3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012315; Expressed in kidney and 16 other tissues.
DR Genevisible; Q0D2L3; RN.
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 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; PS51409; ARGINASE_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydrolase; Manganese; Metal-binding; Mitochondrion;
KW Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..353
FT /note="Agmatinase, 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
