ARGI_BACCD
ID ARGI_BACCD Reviewed; 299 AA.
AC P53608;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P78540};
GN Name=rocF;
OS Bacillus caldovelox.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=33931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 411 / NBRC 15315 / YT-F;
RX PubMed=8647285; DOI=10.1016/0014-5793(96)00459-0;
RA Bewley M.C., Lott J.S., Baker E.N., Patchett M.L.;
RT "The cloning, expression and crystallisation of a thermostable arginase.";
RL FEBS Lett. 386:215-218(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH MANGANESE AND
RP ARGININE, COFACTOR, AND SUBUNIT.
RC STRAIN=DSM 411 / NBRC 15315 / YT-F;
RX PubMed=10196128; DOI=10.1016/s0969-2126(99)80056-2;
RA Bewley M.C., Jeffrey P.D., Patchett M.L., Kanyo Z.F., Baker E.N.;
RT "Crystal structures of Bacillus caldovelox arginase in complex with
RT substrate and inhibitors reveal new insights into activation, inhibition
RT and catalysis in the arginase superfamily.";
RL Structure 7:435-448(1999).
CC -!- FUNCTION: Controls arginine catabolism.
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:P78540};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742,
CC ECO:0000269|PubMed:10196128};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:10196128};
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:0000269|PubMed:10196128}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; U48226; AAB06939.1; -; Genomic_DNA.
DR PIR; S68863; S68863.
DR PDB; 1CEV; X-ray; 2.40 A; A/B/C/D/E/F=1-299.
DR PDB; 2CEV; X-ray; 2.15 A; A/B/C/D/E/F=1-299.
DR PDB; 3CEV; X-ray; 2.40 A; A/B/C/D/E/F=1-299.
DR PDB; 4CEV; X-ray; 2.70 A; A/B/C/D/E/F=1-299.
DR PDB; 5CEV; X-ray; 2.50 A; A/B/C/D/E/F=1-299.
DR PDBsum; 1CEV; -.
DR PDBsum; 2CEV; -.
DR PDBsum; 3CEV; -.
DR PDBsum; 4CEV; -.
DR PDBsum; 5CEV; -.
DR AlphaFoldDB; P53608; -.
DR SMR; P53608; -.
DR DrugBank; DB00536; Guanidine.
DR BRENDA; 3.5.3.1; 644.
DR SABIO-RK; P53608; -.
DR UniPathway; UPA00158; UER00270.
DR EvolutionaryTrace; P53608; -.
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 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..299
FT /note="Arginase"
FT /id="PRO_0000173714"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV"
FT BINDING 124..128
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 226
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV,
FT ECO:0007744|PDB:5CEV"
FT BINDING 226
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV"
FT BINDING 228
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV,
FT ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:3CEV"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10196128,
FT ECO:0007744|PDB:3CEV, ECO:0007744|PDB:5CEV"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1CEV"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2CEV"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1CEV"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:2CEV"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2CEV"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1CEV"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2CEV"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2CEV"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:2CEV"
SQ SEQUENCE 299 AA; 32433 MW; 32D522AFE7F059D1 CRC64;
MKPISIIGVP MDLGQTRRGV DMGPSAMRYA GVIERLERLH YDIEDLGDIP IGKAERLHEQ
GDSRLRNLKA VAEANEKLAA AVDQVVQRGR FPLVLGGDHS IAIGTLAGVA KHYERLGVIW
YDAHGDVNTA ETSPSGNIHG MPLAASLGFG HPALTQIGGY SPKIKPEHVV LIGVRSLDEG
EKKFIREKGI KIYTMHEVDR LGMTRVMEET IAYLKERTDG VHLSLDLDGL DPSDAPGVGT
PVIGGLTYRE SHLAMEMLAE AQIITSAEFV EVNPILDERN KTASVAVALM GSLFGEKLM
