GGH_MYCHD
ID GGH_MYCHD Reviewed; 446 AA.
AC K5BDL0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Glucosylglycerate hydrolase {ECO:0000303|PubMed:25341489};
DE Short=GG hydrolase {ECO:0000303|PubMed:25341489};
DE EC=3.2.1.208 {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
GN Name=ggh {ECO:0000303|PubMed:25341489};
GN ORFNames=C731_0006 {ECO:0000312|EMBL:EKF25940.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=23209251; DOI=10.1128/jb.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=25341489; DOI=10.1038/srep06766;
RA Alarico S., Costa M., Sousa M.S., Maranha A., Lourenco E.C., Faria T.Q.,
RA Ventura M.R., Empadinhas N.;
RT "Mycobacterium hassiacum recovers from nitrogen starvation with up-
RT regulation of a novel glucosylglycerate hydrolase and depletion of the
RT accumulated glucosylglycerate.";
RL Sci. Rep. 4:6766-6766(2014).
RN [3]
RP SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=28876234; DOI=10.1107/s2053230x17012419;
RA Cereija T.B., Alarico S., Empadinhas N., Pereira P.J.B.;
RT "Production, crystallization and structure determination of a mycobacterial
RT glucosylglycerate hydrolase.";
RL Acta Crystallogr. F Struct. Biol. Commun. 73:536-540(2017).
RN [4] {ECO:0007744|PDB:6G3N}
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
RA Cereija T.B., Alarico S., Lourenco E.C., Ventura R., Empadinhas N.,
RA Macedo-Ribeiro S., Pereira P.J.B.;
RT "Structural characterization of mycobacterial hydrolase.";
RL Submitted (MAR-2018) to the PDB data bank.
RN [5] {ECO:0007744|PDB:5OHC, ECO:0007744|PDB:5OHZ, ECO:0007744|PDB:5OI0, ECO:0007744|PDB:5OI1, ECO:0007744|PDB:5OIE, ECO:0007744|PDB:5OIV, ECO:0007744|PDB:5OIW, ECO:0007744|PDB:5OJ4, ECO:0007744|PDB:5OJU, ECO:0007744|PDB:5OJV, ECO:0007744|PDB:5ONT}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-43;
RP ALA-182 AND ALA-419 IN COMPLEXES WITH SERINE; GLUCOSYLGLYCERATE AND
RP MANNOSYLGLYCERATE, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF ASP-43; ASP-182 AND
RP GLU-419, AND ACTIVE SITE.
RX PubMed=31316802; DOI=10.1107/s2052252519005372;
RA Cereija T.B., Alarico S., Lourenco E.C., Manso J.A., Ventura R.,
RA Empadinhas N., Macedo-Ribeiro S., Pereira P.J.B.;
RT "The structural characterization of a glucosylglycerate hydrolase provides
RT insights into the molecular mechanism of mycobacterial recovery from
RT nitrogen starvation.";
RL IUCrJ 6:572-585(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of glucosylglycerate (GG) to
CC glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in
CC recovery from nitrogen starvation by promoting the rapid mobilization
CC of the glucosylglycerate that accumulates under these conditions
CC (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with
CC tenfold lower efficiency (PubMed:31316802).
CC {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)-
CC glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510;
CC EC=3.2.1.208; Evidence={ECO:0000269|PubMed:25341489,
CC ECO:0000269|PubMed:31316802};
CC -!- ACTIVITY REGULATION: Activity is not dependent on divalent cations, but
CC it is enhanced by Mg(2+). {ECO:0000269|PubMed:25341489}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally
CC tagged variant) {ECO:0000269|PubMed:25341489};
CC KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally
CC tagged variant) {ECO:0000269|PubMed:25341489};
CC KM=11.2 mM for glucosylglycerate (at 50 degrees Celsius, C-terminally
CC tagged variant) {ECO:0000269|PubMed:25341489};
CC Vmax=13.7 umol/min/mg enzyme with glucosylglycerate as substrate (at
CC 37 degrees Celsius, C-terminally tagged variant)
CC {ECO:0000269|PubMed:25341489};
CC Vmax=15.2 umol/min/mg enzyme with glucosylglycerate as substrate (at
CC 42 degrees Celsius, C-terminally tagged variant)
CC {ECO:0000269|PubMed:25341489};
CC Vmax=12.3 umol/min/mg enzyme with glucosylglycerate as substrate (at
CC 50 degrees Celsius, C-terminally tagged variant)
CC {ECO:0000269|PubMed:25341489};
CC Vmax=3.60 umol/min/mg enzyme with glucosylglycerate as substrate (at
CC 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802};
CC Vmax=3.09 umol/min/mg enzyme with mannosylglycerate as substrate (at
CC 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802};
CC pH dependence:
CC Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is
CC 5.8 (C-terminally tagged variant) (PubMed:25341489).
CC {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
CC Temperature dependence:
CC Optimum temperature is 50-55 degrees Celsius (tag-less variant)
CC (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C-
CC terminally tagged variant) (PubMed:25341489).
CC {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:28876234,
CC ECO:0000269|PubMed:31316802}.
CC -!- INDUCTION: Up-regulated in response to nitrogen shock.
CC {ECO:0000269|PubMed:25341489}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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DR EMBL; AMRA01000001; EKF25940.1; -; Genomic_DNA.
DR RefSeq; WP_005623031.1; NZ_LR026975.1.
DR PDB; 5OHC; X-ray; 2.00 A; A/B=1-446.
DR PDB; 5OHZ; X-ray; 2.04 A; A/B/C/D=1-446.
DR PDB; 5OI0; X-ray; 1.68 A; A/B=1-446.
DR PDB; 5OI1; X-ray; 1.75 A; A/B=1-446.
DR PDB; 5OIE; X-ray; 2.07 A; A/B=1-446.
DR PDB; 5OIV; X-ray; 1.78 A; A/B=1-446.
DR PDB; 5OIW; X-ray; 1.71 A; A/B=1-446.
DR PDB; 5OJ4; X-ray; 1.79 A; A/B=1-446.
DR PDB; 5OJU; X-ray; 2.17 A; A/B=1-446.
DR PDB; 5OJV; X-ray; 2.06 A; A/B=1-446.
DR PDB; 5ONT; X-ray; 2.05 A; A/B=1-446.
DR PDB; 5ONZ; X-ray; 1.93 A; A/B=1-446.
DR PDB; 5OO2; X-ray; 2.06 A; A/B=1-446.
DR PDB; 6G3N; X-ray; 2.32 A; A/B=1-446.
DR PDB; 6Q5T; X-ray; 2.54 A; A/B=1-446.
DR PDBsum; 5OHC; -.
DR PDBsum; 5OHZ; -.
DR PDBsum; 5OI0; -.
DR PDBsum; 5OI1; -.
DR PDBsum; 5OIE; -.
DR PDBsum; 5OIV; -.
DR PDBsum; 5OIW; -.
DR PDBsum; 5OJ4; -.
DR PDBsum; 5OJU; -.
DR PDBsum; 5OJV; -.
DR PDBsum; 5ONT; -.
DR PDBsum; 5ONZ; -.
DR PDBsum; 5OO2; -.
DR PDBsum; 6G3N; -.
DR PDBsum; 6Q5T; -.
DR AlphaFoldDB; K5BDL0; -.
DR SMR; K5BDL0; -.
DR STRING; 1122247.C731_0006; -.
DR EnsemblBacteria; EKF25940; EKF25940; C731_0006.
DR PATRIC; fig|1122247.3.peg.6; -.
DR eggNOG; COG1626; Bacteria.
DR OMA; NSPRWDS; -.
DR OrthoDB; 70058at2; -.
DR BRENDA; 3.2.1.208; 15810.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:InterPro.
DR GO; GO:0102547; F:glucosylglycerate hydrolase activity; IEA:RHEA.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome; Stress response.
FT CHAIN 1..446
FT /note="Glucosylglycerate hydrolase"
FT /id="PRO_0000449938"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:31316802"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:31316802"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 375..376
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31316802"
FT MUTAGEN 43
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31316802"
FT MUTAGEN 182
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31316802"
FT MUTAGEN 419
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31316802"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6Q5T"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5ONT"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5OJ4"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 135..162
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 253..272
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 347..351
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:5OHC"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5OJU"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5OI0"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:5OI0"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5OI0"
FT HELIX 435..445
FT /evidence="ECO:0007829|PDB:5OI0"
SQ SEQUENCE 446 AA; 50769 MW; E7856A89CE5665AB CRC64;
MPHDPSFTPT QLAARAAYLL RGNDLGTMTT AAPLLYPHMW SWDAAFVAIG LAPLSVERAV
VELDTLLSAQ WRNGMIPHIV FANGVDGYFP GPARWATATL ADNAPRNRLT SGITQPPVHA
IAVQRILEHA RTRGRSTRAV AEAFLDRRWG DLMRWHRWLA ECRDRNERGR ITLYHGWESG
MDNSPRWDSA YANVVPGKLP EYQRADNVII TDPSQRPSDG EYDRYLWLLE EMKAVRYDDE
RLPSVMSFQV EDVFFSAIFS VACQVLAEIG EDYKRPHADV KDLYLWAERF RAGVVETTDQ
RTGAARDFDV LAEKWLVTET AAQFAPLLCG GLPHDRERAL LKLLEGPRFC GHPDLKYGLI
PSTSPVSRDF RPREYWRGPV WPVLTWLFSW CFARRGWAER ARLLRQEGLR QASDGSFAEY
YEPFTGEPLG SMQQSWTAAA VLDWLG
