UDG_CAMJE
ID UDG_CAMJE Reviewed; 393 AA.
AC Q0P8H3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000255|PIRNR:PIRNR000124, ECO:0000303|PubMed:33621065};
DE Short=UDP-Glc dehydrogenase {ECO:0000305};
DE Short=UDP-GlcDH {ECO:0000305};
DE Short=UDPGDH {ECO:0000305};
DE EC=1.1.1.22 {ECO:0000255|PIRNR:PIRNR000124, ECO:0000269|PubMed:33621065};
GN Name=kfiD {ECO:0000312|EMBL:CAL35550.1};
GN OrderedLocusNames=Cj1441c {ECO:0000312|EMBL:CAL35550.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000312|EMBL:CAL35550.1};
RN [1] {ECO:0000312|EMBL:CAL35550.1, ECO:0000312|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000312|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2] {ECO:0007744|PDB:7KWS}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH NAD AND UDP-GLUCOSE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, ACTIVE SITE, AND REACTION MECHANISM.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:33621065};
RX PubMed=33621065; DOI=10.1021/acs.biochem.0c00953;
RA Riegert A.S., Raushel F.M.;
RT "Functional and Structural Characterization of the UDP-Glucose
RT Dehydrogenase Involved in Capsular Polysaccharide Biosynthesis from
RT Campylobacter jejuni.";
RL Biochemistry 60:725-734(2021).
CC -!- FUNCTION: Catalyzes the formation of UDP-glucuronic acid which is
CC required for capsular polysaccharide synthesis. Does not catalyze the
CC formation of glucuronamide moiety of the capsular polysaccharide.
CC {ECO:0000269|PubMed:33621065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000255|PIRNR:PIRNR000124,
CC ECO:0000269|PubMed:33621065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for UDP-glucose (at pH 8.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:33621065};
CC KM=190 uM for NAD(+) (at pH 8.7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:33621065};
CC Note=kcat is 1.2 sec(-1) with UDP-glucose as substrate. kcat is 0.80
CC sec(-1) with NAD(+) as substrate. {ECO:0000269|PubMed:33621065};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000269|PubMed:33621065}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:33621065}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:33621065}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000255|PIRNR:PIRNR000124}.
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DR EMBL; AL111168; CAL35550.1; -; Genomic_DNA.
DR PIR; A81290; A81290.
DR RefSeq; WP_002851145.1; NC_002163.1.
DR RefSeq; YP_002344824.1; NC_002163.1.
DR PDB; 7KWS; X-ray; 2.09 A; A/B=1-393.
DR PDBsum; 7KWS; -.
DR AlphaFoldDB; Q0P8H3; -.
DR SMR; Q0P8H3; -.
DR IntAct; Q0P8H3; 10.
DR STRING; 192222.Cj1441c; -.
DR PaxDb; Q0P8H3; -.
DR PRIDE; Q0P8H3; -.
DR EnsemblBacteria; CAL35550; CAL35550; Cj1441c.
DR GeneID; 905730; -.
DR KEGG; cje:Cj1441c; -.
DR PATRIC; fig|192222.6.peg.1422; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_2_0_7; -.
DR OMA; EDFTRPD; -.
DR BRENDA; 1.1.1.22; 13746.
DR UniPathway; UPA00038; UER00491.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IC:UniProtKB.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028357; UDPglc_DH_bac.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500134; UDPglc_DH_bac; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..393
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000454940"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-1,
FT ECO:0000305|PubMed:33621065"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 143..147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 244..248
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:33621065,
FT ECO:0007744|PDB:7KWS"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR500134-3,
FT ECO:0000269|PubMed:33621065, ECO:0007744|PDB:7KWS"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7KWS"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 192..222
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:7KWS"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 274..295
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:7KWS"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:7KWS"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:7KWS"
SQ SEQUENCE 393 AA; 45093 MW; 31F9A1E96743C1B3 CRC64;
MKIVIVGIGY VGLANAILFS KNNENEVVLL DIDENKIQSI NNHKSPIKDK LIEKFFVQNI
SKLHATSNIK EAYFNADFAV IATPTDYDEQ LNFFDTRSIE NVLKDIKNIN SKINVIIKST
VPIGYTKTIK QKFNMSNIVF SPEFLREGSA LYDSLYPSRI IIGDKSVLGK TIGDLFLKNI
EKKNVDIFYM DSDEAESVKL FSNTYLAMRV GFFNEVDSYA RKHNLNSADI IKGISADDRI
GKYYNNPSFG YGGYCLPKDT KQLLANFYNI PNSLIKAIVE TNEIRKKFIT QLILEKKPNI
LGIYRLIMKQ NSDNFRNSVI IDIIKYLQEY NSNIELIIYE PLVKEKKFLN IKVENDFNVF
GAKVDLIIAN RFDDKLKEIK DKVFSADVFY TDI
