ARGI_BACSU
ID ARGI_BACSU Reviewed; 296 AA.
AC P39138;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000269|PubMed:7540694};
GN Name=rocF {ECO:0000303|PubMed:7540694}; OrderedLocusNames=BSU40320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ARGINASE AND IN ARGININE
RP CATABOLISM, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=7540694; DOI=10.1006/jmbi.1995.0342;
RA Gardan R., Rapoport G., Debarbouille M.;
RT "Expression of the rocDEF operon involved in arginine catabolism in
RT Bacillus subtilis.";
RL J. Mol. Biol. 249:843-856(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION.
RX PubMed=104957; DOI=10.1128/jb.137.1.189-196.1979;
RA Baumberg S., Harwood C.R.;
RT "Carbon and nitrogen repression of arginine catabolic enzymes in Bacillus
RT subtilis.";
RL J. Bacteriol. 137:189-196(1979).
CC -!- FUNCTION: Involved in the catabolism of arginine.
CC {ECO:0000269|PubMed:7540694}.
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; Evidence={ECO:0000269|PubMed:7540694};
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 -!- INDUCTION: Part of the rocDEF operon. Expression is sigma L dependent,
CC induced by arginine, ornithine or proline. {ECO:0000269|PubMed:104957,
CC ECO:0000269|PubMed:7540694}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on arginine
CC as a sole nitrogen source, but do grow on ornithine or ammonium
CC chloride. {ECO:0000269|PubMed:7540694}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; X81802; CAA57400.1; -; Genomic_DNA.
DR EMBL; D78193; BAA11291.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16069.1; -; Genomic_DNA.
DR PIR; S55795; S55795.
DR RefSeq; NP_391912.1; NC_000964.3.
DR RefSeq; WP_003226959.1; NZ_JNCM01000034.1.
DR PDB; 6DKT; X-ray; 2.08 A; A/B/C/D/E/F=1-296.
DR PDB; 6NFP; X-ray; 1.70 A; A/B/C/D/E/F=1-296.
DR PDBsum; 6DKT; -.
DR PDBsum; 6NFP; -.
DR AlphaFoldDB; P39138; -.
DR SMR; P39138; -.
DR STRING; 224308.BSU40320; -.
DR jPOST; P39138; -.
DR PaxDb; P39138; -.
DR PRIDE; P39138; -.
DR EnsemblBacteria; CAB16069; CAB16069; BSU_40320.
DR GeneID; 937760; -.
DR KEGG; bsu:BSU40320; -.
DR PATRIC; fig|224308.179.peg.4362; -.
DR eggNOG; COG0010; Bacteria.
DR InParanoid; P39138; -.
DR OMA; IATCFGQ; -.
DR PhylomeDB; P39138; -.
DR BioCyc; BSUB:BSU40320-MON; -.
DR BRENDA; 3.5.3.1; 658.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004053; F:arginase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Arginase"
FT /id="PRO_0000173715"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 122..126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 66..85
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:6NFP"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:6NFP"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6NFP"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:6NFP"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6NFP"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:6NFP"
SQ SEQUENCE 296 AA; 32154 MW; A4074652A0B6C80D CRC64;
MDKTISVIGM PMDLGQARRG VDMGPSAIRY AHLIERLSDM GYTVEDLGDI PINREKIKND
EELKNLNSVL AGNEKLAQKV NKVIEEKKFP LVLGGDHSIA IGTLAGTAKH YDNLGVIWYD
AHGDLNTLET SPSGNIHGMP LAVSLGIGHE SLVNLEGYAP KIKPENVVII GARSLDEGER
KYIKESGMKV YTMHEIDRLG MTKVIEETLD YLSACDGVHL SLDLDGLDPN DAPGVGTPVV
GGISYRESHL AMEMLYDAGI ITSAEFVEVN PILDHKNKTG KTAVELVESL LGKKLL
