ARGI_AGRFC
ID ARGI_AGRFC Reviewed; 324 AA.
AC P14012;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=arcA; Synonyms=arc; OrderedLocusNames=Atu6018; ORFNames=AGR_pTi_56;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OG Plasmid pTiC58.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2806247; DOI=10.1111/j.1432-1033.1989.tb15060.x;
RA Schrell A., Alt-Moerbe J., Lanz T., Schroeder J.;
RT "Arginase of Agrobacterium Ti plasmid C58. DNA sequence, properties, and
RT comparison with eucaryotic enzymes.";
RL Eur. J. Biochem. 184:635-641(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3040404; DOI=10.1111/j.1432-1033.1987.tb13306.x;
RA Sans N., Schroeder G., Schroeder J.;
RT "The Noc region of Ti plasmid C58 codes for arginase and ornithine
RT cyclodeaminase.";
RL Eur. J. Biochem. 167:81-87(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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: Homohexamer. {ECO:0000305}.
CC -!- INDUCTION: By nopaline. But not by L-arginine or L-ornithine.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15884; CAA33894.1; -; Genomic_DNA.
DR EMBL; Z30316; CAA82964.1; -; Genomic_DNA.
DR EMBL; AE007871; AAK90976.2; -; Genomic_DNA.
DR PIR; AH3229; AH3229.
DR PIR; S06118; S06118.
DR RefSeq; NP_396535.2; NC_003065.3.
DR RefSeq; WP_010891454.1; NC_003065.3.
DR AlphaFoldDB; P14012; -.
DR SMR; P14012; -.
DR EnsemblBacteria; AAK90976; AAK90976; Atu6018.
DR KEGG; atu:Atu6018; -.
DR PATRIC; fig|176299.10.peg.5225; -.
DR HOGENOM; CLU_039478_6_2_5; -.
DR OMA; EMARSCD; -.
DR PhylomeDB; P14012; -.
DR BioCyc; AGRO:ATU6018-MON; -.
DR BioCyc; MetaCyc:MON-11552; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000000813; Plasmid Ti.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..324
FT /note="Arginase"
FT /id="PRO_0000173712"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 144..148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 155..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
SQ SEQUENCE 324 AA; 34695 MW; 6719BFF66B80571D CRC64;
MNGAGEINAS RHRKENELKT CQILGAPVQS GASQPGCLMG PDAFRTAGLT QVLTELGWAV
TDLGDATPTV EPELSHPNSA VKNLDALVGW TRSLSQKALE MARSCDLPVF LGGDHSMSAG
TVSGVAQRTA ELGKEQFVLW LDAHTDLHTL HTTASGNLHG TPVAYYTGQS GFEGLPPLAA
PVNPRNVSMM GIRSVDPEER RRVAEIGVQV ADMRVLDEQG VVRPLEAFLD RVSKVSGRLH
VSLDVDFLDP AIAPAVGTTV PGGATFREAH LIMEMLHDSG LVTSLDLAEL NPFLDERGRT
ARLITDLASS LFGRRVFDRV TTAF
