AGUA_CELJU
ID AGUA_CELJU Reviewed; 732 AA.
AC B3PC73; Q8VP74;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Extracellular xylan exo-alpha-(1->2)-glucuronosidase;
DE EC=3.2.1.131;
DE AltName: Full=Alpha-glucuronidase;
DE Flags: Precursor;
GN Name=gla67A; Synonyms=glcA67A; OrderedLocusNames=CJA_2887;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12169619; DOI=10.1128/jb.184.17.4925-4929.2002;
RA Nagy T., Emami K., Fontes C.M., Ferreira L.M., Humphry D.R., Gilbert H.J.;
RT "The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa
RT hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-
RT glucuronoxylan.";
RL J. Bacteriol. 184:4925-4929(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 25-732 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, FUNCTION, MUTAGENESIS OF GLU-312; ASP-385 AND GLU-413, ACTIVE
RP SITE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=11937059; DOI=10.1016/s0969-2126(02)00742-6;
RA Nurizzo D., Nagy T., Gilbert H.J., Davies G.J.;
RT "The structural basis for catalysis and specificity of the Pseudomonas
RT cellulosa alpha-glucuronidase, GlcA67A.";
RL Structure 10:547-556(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 25-732 OF MUTANT ALA-312 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF TRP-180; VAL-230;
RP ARG-345; LYS-380 AND TRP-563, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=12654910; DOI=10.1074/jbc.m302205200;
RA Nagy T., Nurizzo D., Davies G.J., Biely P., Lakey J.H., Bolam D.N.,
RA Gilbert H.J.;
RT "The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the
RT carboxylate and methyl groups of aldobiouronic acid as important substrate
RT recognition determinants.";
RL J. Biol. Chem. 278:20286-20292(2003).
CC -!- FUNCTION: Alpha-glucuronidase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic
CC bond at the non-reducing end of 4-O-methyl-D-glucuronic acid (4-O-
CC MeGlcA) side chain of short xylooligosaccharides and releases 4-O-
CC methylglucuronic acid. It can also hydrolyze small soluble
CC oligosaccharides such as dobiouronic acid, aldotriouronic acid,
CC aldotetraouronic acid, and aldopentaouronic acid.
CC {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12169619,
CC ECO:0000269|PubMed:12654910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in
CC the main chain of hardwood xylans.; EC=3.2.1.131;
CC Evidence={ECO:0000269|PubMed:12169619};
CC -!- ACTIVITY REGULATION: Inhibited by 4-O-MeGlcA.
CC {ECO:0000269|PubMed:12654910}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for aldotriouronic acid (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910};
CC KM=0.36 mM for aldotetraouronic acid (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910};
CC KM=0.42 mM for aldopentaouronic acid (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910};
CC KM=0.53 mM for aldobiouronic acid (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11937059,
CC ECO:0000269|PubMed:12169619, ECO:0000269|PubMed:12654910}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:12169619}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY065638; AAL57752.1; -; Genomic_DNA.
DR EMBL; CP000934; ACE83468.1; -; Genomic_DNA.
DR RefSeq; WP_012488471.1; NC_010995.1.
DR PDB; 1GQI; X-ray; 1.48 A; A/B=25-732.
DR PDB; 1GQJ; X-ray; 1.90 A; A/B=25-732.
DR PDB; 1GQK; X-ray; 1.90 A; A/B=25-732.
DR PDB; 1GQL; X-ray; 1.67 A; A/B=25-732.
DR PDB; 1H41; X-ray; 1.50 A; A/B=25-732.
DR PDBsum; 1GQI; -.
DR PDBsum; 1GQJ; -.
DR PDBsum; 1GQK; -.
DR PDBsum; 1GQL; -.
DR PDBsum; 1H41; -.
DR AlphaFoldDB; B3PC73; -.
DR SMR; B3PC73; -.
DR STRING; 498211.CJA_2887; -.
DR CAZy; GH67; Glycoside Hydrolase Family 67.
DR EnsemblBacteria; ACE83468; ACE83468; CJA_2887.
DR KEGG; cja:CJA_2887; -.
DR eggNOG; COG3661; Bacteria.
DR HOGENOM; CLU_007125_1_0_6; -.
DR OMA; DNNGWGQ; -.
DR OrthoDB; 207695at2; -.
DR BRENDA; 3.2.1.139; 5103.
DR SABIO-RK; B3PC73; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IDA:UniProtKB.
DR GO; GO:2000886; P:glucuronoxylan catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.379.10; -; 1.
DR Gene3D; 3.90.1330.10; -; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell outer membrane; Glycosidase;
KW Hydrolase; Membrane; Polysaccharide degradation; Reference proteome;
KW Signal; Xylan degradation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..732
FT /note="Extracellular xylan exo-alpha-(1->2)-
FT glucuronosidase"
FT /id="PRO_0000422176"
FT ACT_SITE 312
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11937059"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11937059"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11937059"
FT BINDING 188..189
FT /ligand="substrate"
FT BINDING 231
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT BINDING 308
FT /ligand="substrate"
FT BINDING 345
FT /ligand="substrate"
FT BINDING 356
FT /ligand="substrate"
FT BINDING 380
FT /ligand="substrate"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="substrate"
FT BINDING 563
FT /ligand="substrate"
FT SITE 180
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT SITE 563
FT /note="Participates in a stacking interactions with the
FT sugar rings of 4-O-MeGlcA"
FT MUTAGEN 180
FT /note="W->A: Greatly reduced the glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 230
FT /note="V->A: No influence on the glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 230
FT /note="V->G: Little influence on the glucuronosidase
FT activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 230
FT /note="V->N: Considerably less active than wild-type."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 230
FT /note="V->S: Considerably less active than wild-type."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 308
FT /note="K->A: Greatly reduced the glucuronosidase activity."
FT MUTAGEN 312
FT /note="E->A: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 312
FT /note="E->C: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 345
FT /note="R->A: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 380
FT /note="K->A: Greatly reduced the glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT MUTAGEN 385
FT /note="D->A: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 385
FT /note="D->C: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 413
FT /note="E->A: Loss of glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 413
FT /note="E->C: Retains 20% of the of glucuronosidase
FT activity."
FT /evidence="ECO:0000269|PubMed:11937059"
FT MUTAGEN 563
FT /note="W->A: Greatly reduced the glucuronosidase activity."
FT /evidence="ECO:0000269|PubMed:12654910"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 375..386
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 413..419
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 445..450
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 479..491
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 513..532
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 582..585
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:1GQI"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 607..612
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 628..651
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 652..656
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 659..691
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 706..715
FT /evidence="ECO:0007829|PDB:1GQI"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:1GQI"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:1GQI"
SQ SEQUENCE 732 AA; 83021 MW; E3219C0AB50E7685 CRC64;
MSTFARLFLC LVFFASLQPA MAQTEDGYDM WLRYQPIADQ TLLKTYQKQI RHLHVAGDSP
TINAAAAELQ RGLSGLLNKP IVARDEKLKD YSLVIGTPDN SPLIASLNLG ERLQALGAEG
YLLEQTRINK RHVVIVAANS DVGVLYGSFH LLRLIQTQHA LEKLSLSSAP RLQHRVVNHW
DNLNRVVERG YAGLSLWDWG SLPNYLAPRY TDYARINASL GINGTVINNV NADPRVLSDQ
FLQKIAALAD AFRPYGIKMY LSINFNSPRA FGDVDTADPL DPRVQQWWKT RAQKIYSYIP
DFGGFLVKAD SEGQPGPQGY GRDHAEGANM LAAALKPFGG VVFWRAFVYH PDIEDRFRGA
YDEFMPLDGK FADNVILQIK NGPIDFQPRE PFSALFAGMS RTNMMMEFQI TQEYFGFATH
LAYQGPLFEE SLKTETHARG EGSTIGNILE GKVFKTRHTG MAGVINPGTD RNWTGHPFVQ
SSWYAFGRMA WDHQISAATA ADEWLRMTFS NQPAFIEPVK QMMLVSREAG VNYRSPLGLT
HLYSQGDHYG PAPWTDDLPR ADWTAVYYHR ASKTGIGFNR TKTGSNALAQ YPEPIAKAWG
DLNSVPEDLI LWFHHLSWDH RMQSGRNLWQ ELVHKYYQGV EQVRAMQRTW DQQEAYVDAA
RFAQVKALLQ VQEREAVRWR NSCVLYFQSV AGRPIPANYE QPEHDLEYYK MLARTTYVPE
PWHPASSSRV LK
