GUDX_ECOLI
ID GUDX_ECOLI Reviewed; 446 AA.
AC Q46915; Q2MA46;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glucarate dehydratase-related protein;
DE Short=GDH-RP;
DE Short=GlucDRP;
DE EC=4.2.1.-;
GN Name=gudX; Synonyms=ygcY; OrderedLocusNames=b2788, JW2759;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9772162; DOI=10.1021/bi981124f;
RA Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily:
RT characterization of the (D)-glucarate/galactarate catabolic pathway in
RT Escherichia coli.";
RL Biochemistry 37:14369-14375(1998).
CC -!- FUNCTION: Does not seem to have an in-vivo activity on glucarate or
CC idarate. Its real substrate is unknown.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 uM for idarate {ECO:0000269|PubMed:9772162};
CC KM=320 uM for glucarate {ECO:0000269|PubMed:9772162};
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GlucD subfamily. {ECO:0000305}.
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DR EMBL; U29581; AAB40438.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75830.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76860.1; -; Genomic_DNA.
DR PIR; H65060; H65060.
DR RefSeq; NP_417268.1; NC_000913.3.
DR RefSeq; WP_000235391.1; NZ_LN832404.1.
DR PDB; 4GYP; X-ray; 2.10 A; C/D=2-446.
DR PDB; 4IL0; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-446.
DR PDBsum; 4GYP; -.
DR PDBsum; 4IL0; -.
DR AlphaFoldDB; Q46915; -.
DR SMR; Q46915; -.
DR BioGRID; 4260899; 21.
DR IntAct; Q46915; 3.
DR STRING; 511145.b2788; -.
DR PaxDb; Q46915; -.
DR PRIDE; Q46915; -.
DR EnsemblBacteria; AAC75830; AAC75830; b2788.
DR EnsemblBacteria; BAE76860; BAE76860; BAE76860.
DR GeneID; 947261; -.
DR KEGG; ecj:JW2759; -.
DR KEGG; eco:b2788; -.
DR PATRIC; fig|1411691.4.peg.3946; -.
DR EchoBASE; EB2960; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_9_0_6; -.
DR InParanoid; Q46915; -.
DR OMA; WGRFVRT; -.
DR PhylomeDB; Q46915; -.
DR BioCyc; EcoCyc:G7446-MON; -.
DR SABIO-RK; Q46915; -.
DR PRO; PR:Q46915; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; ISS:EcoCyc.
DR CDD; cd03323; D-glucarate_dehydratase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR034598; GlucD-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00005; glucarate_dehydratase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Glucarate dehydratase-related protein"
FT /id="PRO_0000171266"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338..340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 8..20
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4IL0"
FT HELIX 107..127
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4IL0"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:4GYP"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4GYP"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:4GYP"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4GYP"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 403..414
FT /evidence="ECO:0007829|PDB:4GYP"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:4GYP"
SQ SEQUENCE 446 AA; 48850 MW; 9010C7FAAE4FBE49 CRC64;
MATQSSPVIT DMKVIPVAGH DSMLLNIGGA HNAYFTRNIV VLTDNAGHTG IGEAPGGDVI
YQTLVDAIPM VLGQEVARLN KVVQQVHKGN QAADFDTFGK GAWTFELRVN AVAALEAALL
DLLGKALNVP VCELLGPGKQ REAITVLGYL FYIGDRTKTD LPYVENTPGN HEWYQLRHQK
AMNSEAVVRL AEASQDRYGF KDFKLKGGVL PGEQEIDTVR ALKKRFPDAR ITVDPNGAWL
LDEAISLCKG LNDVLTYAED PCGAEQGFSG REVMAEFRRA TGLPVATNMI ATNWREMGHA
VMLNAVDIPL ADPHFWTLSG AVRVAQLCDD WGLTWGCHSN NHFDISLAMF THVGAAAPGN
PTAIDTHWIW QEGDCRLTQN PLEIKNGKIA VPDAPGLGVE LDWEQVQKAH EAYKRLPGGA
RNDAGPMQYL IPGWTFDRKR PVFGRH
