ARGI_LITCT
ID ARGI_LITCT Reviewed; 323 AA.
AC P49900;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Arginase, hepatic;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Atkinson B.G., Helbing C.C., Chen Y.;
RT "Reprogramming of gene expression in the liver of Rana catesbeiana tadpoles
RT during spontaneous and thyroid hormone induced metamorphosis.";
RL (In) Davey K.G., Peter R.E., Tobe S.S. (eds.);
RL Perspectives in comparative endocrinology, pp.416-423, National Research
RL Council of Canada, Ottawa (1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7841190; DOI=10.1016/0167-4781(94)00183-4;
RA Iwase K., Yamauchi K., Ishikawa K.;
RT "Cloning of cDNAs encoding argininosuccinate lyase and arginase from Rana
RT catesbeiana liver and regulation of their mRNAs during spontaneous and
RT thyroid hormone-induced metamorphosis.";
RL Biochim. Biophys. Acta 1260:139-146(1995).
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:P05089};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {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:P05089}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; U26351; AAA68073.1; -; mRNA.
DR EMBL; D38303; BAA07422.1; -; mRNA.
DR PIR; S52134; S52134.
DR AlphaFoldDB; P49900; -.
DR SMR; P49900; -.
DR UniPathway; UPA00158; UER00270.
DR GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 2: Evidence at transcript level;
KW Arginine metabolism; Hydrolase; Manganese; Metal-binding; Urea cycle.
FT CHAIN 1..323
FT /note="Arginase, hepatic"
FT /id="PRO_0000173702"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 127..131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 138..140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P78540"
FT CONFLICT 316..321
FT /note="SLRVPD -> ICVF (in Ref. 2; BAA07422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 35293 MW; FD8167DF02C69583 CRC64;
MSERTKRSVG VLGAPFSKGQ ARGGVEEGPI YIRRAGLIEK LEELEYEVRD YGDLHFPELP
CDEPFQNVKN PRTVGQAAEK VANAVSEVKR SGRVCLTLGG DHSLAVGTIT GHAKVHPDLC
VVWVDAHADI NTPITSPSGN LHGQPVSFLI RELQTKVPAI PGFSWVQPSL SAKDIVYIGL
RDVDPGEHYI LKTLGIKSYS MSDVDRLTIN KVMEETIEFL VGKKKRPIHL SFDIDGLDPS
VAPATGTPVP GGLTYREGMY ITEQLYNTGL LSAVDMMEVN PSRGETERES KLTVNTSLNM
ILSCFGKARE GFHASSLRVP DLI
