GBH_ARTS8
ID GBH_ARTS8 Reviewed; 353 AA.
AC Q8KZT5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Guanidinobutyrase;
DE Short=GBase;
DE EC=3.5.3.7;
DE AltName: Full=D-arginase;
DE EC=3.5.3.10;
GN Name=gbh;
OS Arthrobacter sp. (strain KUJ 8602).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=196628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13; 41-54; 237-252
RP AND 312-325, AND CHARACTERIZATION.
RX PubMed=12761196; DOI=10.1093/jb/mvg016;
RA Arakawa N., Igarashi M., Kazuoka T., Oikawa T., Soda K.;
RT "D-arginase of Arthrobacter sp. KUJ 8602: characterization and its identity
RT with Zn(2+)-guanidinobutyrase.";
RL J. Biochem. 133:33-42(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-guanidinobutanoate + H2O = 4-aminobutanoate + urea;
CC Xref=Rhea:RHEA:19501, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:57486, ChEBI:CHEBI:59888; EC=3.5.3.7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arginine + H2O = D-ornithine + urea; Xref=Rhea:RHEA:12901,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32689,
CC ChEBI:CHEBI:57668; EC=3.5.3.10;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by 5-aminovalerate, mercaptoacetate, 3-
CC mercaptopropionate and 2-mercaptoethanol.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-9.5 with 4-guanidinobutyrate as substrate, and 9.5-
CC 10 with D-arginine or L-arginine as substrate.;
CC -!- SUBUNIT: Homohexamer.
CC -!- MISCELLANEOUS: Acts in decreasing order on 4-guanidinobutyrate, D-
CC arginine, 3-guanidinopropionate, 5-guanidinovalerate and L-arginine.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00742}.
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DR EMBL; AB085822; BAB96819.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KZT5; -.
DR SMR; Q8KZT5; -.
DR PRIDE; Q8KZT5; -.
DR KEGG; ag:BAB96819; -.
DR BioCyc; MetaCyc:MON-11569; -.
DR BRENDA; 3.5.3.10; 457.
DR BRENDA; 3.5.3.7; 457.
DR GO; GO:0047817; F:D-arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0047971; F:guanidinobutyrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
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; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Zinc.
FT CHAIN 1..353
FT /note="Guanidinobutyrase"
FT /id="PRO_0000173747"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
SQ SEQUENCE 353 AA; 37933 MW; EB2CE94AD6D42D8D CRC64;
MEELRIEANG NLGPIDSSRI PRYAGAATYA RLPRLDQVSK ADVTVVGVPF DSGVSYRPGA
RFGANHVREA SRLLRPYNPA WDVSPFENIQ VADAGDMAVN PFNINEAIET IQQNALDLTA
NGSKLVTLGG DHTIALPLLR AAAERAGEPI AMLHFDAHLD TWDTYFGAEY THGTPFRRAV
EEGILDTEAI SHVGTRGPLY GKKDLDDDHR FGFGIVTSAD VYYQGVLETV AKIRDRIGNR
PLYISVDIDV LDPAHAPGTG TPEAGGITSR ELLEIIRGFR GMNLVGADVV EVAPAYDHAE
ITGVAGSHVA YELVTLMADN AVEGDRHGAP NGYAQQALGA RIQEVAQAIG GQR
