GBU1_KLULA
ID GBU1_KLULA Reviewed; 410 AA.
AC Q6CIB4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Guanidinobutyrase {ECO:0000303|PubMed:24912400};
DE EC=3.5.3.7 {ECO:0000269|PubMed:24912400};
GN Name=GBU1 {ECO:0000303|PubMed:24912400}; OrderedLocusNames=KLLA0F27995g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24912400; DOI=10.1111/mmi.12666;
RA Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R.,
RA van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V.,
RA Wahl S.A., Pronk J.T., Daran J.M.;
RT "An alternative, arginase-independent pathway for arginine metabolism in
RT Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.";
RL Mol. Microbiol. 93:369-389(2014).
CC -!- FUNCTION: Catalyzes the hydrolysis of 4-guanidinobutanoate to gamma-
CC aminobutyrate (GABA) and urea. Involved in an alternative, arginase-
CC independent arginine degradation pathway via GABA.
CC {ECO:0000269|PubMed:24912400}.
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 Evidence={ECO:0000269|PubMed:24912400};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9I3S3,
CC ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q9I3S3,
CC ECO:0000255|PROSITE-ProRule:PRU00742};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation.
CC {ECO:0000305|PubMed:24912400}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000305}.
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DR EMBL; CR382126; CAG99033.1; -; Genomic_DNA.
DR RefSeq; XP_456325.1; XM_456325.1.
DR AlphaFoldDB; Q6CIB4; -.
DR SMR; Q6CIB4; -.
DR STRING; 28985.XP_456325.1; -.
DR EnsemblFungi; CAG99033; CAG99033; KLLA0_F27995g.
DR GeneID; 2895050; -.
DR KEGG; kla:KLLA0_F27995g; -.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_1_1_1; -.
DR InParanoid; Q6CIB4; -.
DR OMA; CIDAGFV; -.
DR BioCyc; MetaCyc:MON-18734; -.
DR UniPathway; UPA00073; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0047971; F:guanidinobutyrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
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 PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..410
FT /note="Guanidinobutyrase"
FT /id="PRO_0000432231"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I3S3"
SQ SEQUENCE 410 AA; 45550 MW; 0670EE0D7F393980 CRC64;
MKVAGFILGA LIQFSLTEGH VEQNENANLT EMWGEDWPFS GIQTFAHLPH HKCLIDMEKK
FDIGVIGVPF DTAVSFRGGA RFGPQAIRKA SQRQTSMRGF NFRADINPYQ DWASVVDCGD
VPVTPMDNCL ALKMMTAAYE NLLSHESQTS DNNLPPRFVT LGGDHSIILP ALRALRKTYG
RLAVIHFDSH LDTWAPSKYP SFWHSDTSEF THGSMLWIAH NEGLLTENNN IHAGLRTRLS
GSSFEDYDDD DKVGFHRIEA DEIMDGGIKS IVEKIKSKIP SDVPVYISVD IDVLDPSAAP
GTGTMEVGGW MTRELIRIIR ELEDLNLVGA DIVEVSPPFD PTEITSLAGA QIAYELITNM
VKKGPIDPEL IKHNLELSDK LTQGQQLLGF SSPTDELNDK IQKEQFVLQA
