URHG1_BACSU
ID URHG1_BACSU Reviewed; 344 AA.
AC O31521;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Unsaturated rhamnogalacturonyl hydrolase YesR;
DE Short=URH;
DE EC=3.2.1.172;
GN Name=yesR; OrderedLocusNames=BSU07000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, MUTAGENESIS OF ASP-135,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16781735; DOI=10.1016/j.jmb.2006.04.047;
RA Itoh T., Ochiai A., Mikami B., Hashimoto W., Murata K.;
RT "A novel glycoside hydrolase family 105: the structure of family 105
RT unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in
RT comparison with family 88 enzyme complexed with the disaccharide.";
RL J. Mol. Biol. 360:573-585(2006).
RN [3]
RP INDUCTION.
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of unsaturated rhamnogalacturonan
CC disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose.
CC It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates
CC containing unsaturated D-glucuronic acid at the non-reducing terminus,
CC although the active pockets of YesR and UGL are very similar.
CC {ECO:0000269|PubMed:16781735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-
CC rhamnose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose;
CC Xref=Rhea:RHEA:30927, ChEBI:CHEBI:15377, ChEBI:CHEBI:17117,
CC ChEBI:CHEBI:62346, ChEBI:CHEBI:62478; EC=3.2.1.172;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=719 uM for unsaturated rhamnogalacturonan disaccharide (at pH 6
CC and 30 degrees Celsius) {ECO:0000269|PubMed:16781735};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:16781735};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. It is stable below 50
CC degrees Celsius. {ECO:0000269|PubMed:16781735};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16781735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 105 family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB12519.1; -; Genomic_DNA.
DR PIR; A69797; A69797.
DR RefSeq; NP_388581.1; NC_000964.3.
DR RefSeq; WP_003243366.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31521; -.
DR SMR; O31521; -.
DR STRING; 224308.BSU07000; -.
DR CAZy; GH105; Glycoside Hydrolase Family 105.
DR PaxDb; O31521; -.
DR PRIDE; O31521; -.
DR DNASU; 938759; -.
DR EnsemblBacteria; CAB12519; CAB12519; BSU_07000.
DR GeneID; 938759; -.
DR KEGG; bsu:BSU07000; -.
DR PATRIC; fig|224308.179.peg.760; -.
DR eggNOG; COG4225; Bacteria.
DR InParanoid; O31521; -.
DR OMA; WAEWAMY; -.
DR PhylomeDB; O31521; -.
DR BioCyc; BSUB:BSU07000-MON; -.
DR BioCyc; MetaCyc:BSU07000-MON; -.
DR BRENDA; 3.2.1.172; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102211; F:unsaturated rhamnogalacturonyl hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010905; Glyco_hydro_88.
DR Pfam; PF07470; Glyco_hydro_88; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16781735"
FT CHAIN 2..344
FT /note="Unsaturated rhamnogalacturonyl hydrolase YesR"
FT /id="PRO_0000364434"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 30..31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 31
FT /note="May be essential to modulate pKa of the D-135
FT carboxyl group"
FT /evidence="ECO:0000250"
FT SITE 74
FT /note="May be essential to modulate pKa of the D-135
FT carboxyl group"
FT /evidence="ECO:0000250"
FT MUTAGEN 135
FT /note="D->N: Loss of hydrolase activity."
FT /evidence="ECO:0000269|PubMed:16781735"
SQ SEQUENCE 344 AA; 38677 MW; 974F7E58504853D2 CRC64;
MAQLIFDEEK VTSVIDRIVK RTFQMDFAWD WPGGVAFYGV AEAYEATENE EYINLLKTWV
DEQLEDGLPP LSINGVSIGH TLLFLHKVTG DDVYLETAAE MAEYVLHKAP RFGEGILQHT
VNAAEYVFPE QAWADTLMMA GLFMLRIGRV MEREDYFEDG LRQFHGHEDV LQDPVTNLYY
HAWDNKAQNH LSGIYWGRAN GWAALTMAKA LPLIEVTHPS FMIIDGSLRD QLSALVRLQD
ESGLWHTILD DPDSYLEVSA SAGIASALMS SGKLYTKYVQ KSLAAILDAV EEDGRVSRVS
AGTAVMKNAE GYKQVPYKRI QGWGQGLALT FLADVLKTKK RLYQ
