GMHD_CAMJE
ID GMHD_CAMJE Reviewed; 313 AA.
AC Q0P8I7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=GDP-D-glycero-alpha-D-manno-heptose dehydrogenase {ECO:0000303|PubMed:32168448};
DE EC=1.1.98.- {ECO:0000269|PubMed:32168448};
GN OrderedLocusNames=Cj1427c {ECO:0000312|EMBL:CAL35536.1};
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:CAL35536.1, ECO:0000312|Proteomes:UP000000799};
RN [1] {ECO:0000312|EMBL:CAL35536.1, 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]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND REACTION MECHANISM.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:32168448};
RX PubMed=32168448; DOI=10.1021/acs.biochem.0c00097;
RA Huddleston J.P., Raushel F.M.;
RT "Functional Characterization of Cj1427, a Unique Ping-Pong Dehydrogenase
RT Responsible for the Oxidation of GDP-d-glycero-alpha-d-manno-heptose in
RT Campylobacter jejuni.";
RL Biochemistry 59:1328-1337(2020).
RN [3] {ECO:0007744|PDB:6VO6, ECO:0007744|PDB:6VO8}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH GDP AND NADH,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:32168450};
RX PubMed=32168450; DOI=10.1021/acs.biochem.0c00096;
RA Huddleston J.P., Anderson T.K., Spencer K.D., Thoden J.B., Raushel F.M.,
RA Holden H.M.;
RT "Structural Analysis of Cj1427, an Essential NAD-Dependent Dehydrogenase
RT for the Biosynthesis of the Heptose Residues in the Capsular
RT Polysaccharides of Campylobacter jejuni.";
RL Biochemistry 59:1314-1327(2020).
CC -!- FUNCTION: NAD-dependent dehydrogenase involved in the biosynthesis of
CC heptose moieties with a hydroxyl group at C6 found on the capsular
CC polysaccharide (CPS) of C.jejuni. Catalyzes the initial oxidation of C4
CC of the GDP-D-glycero-alpha-D-manno-heptose to form GDP-D-glycero-4-
CC keto-alpha-D-lyxo-heptose in the presence of alpha-ketoglutarate
CC required to recycle the NADH nucleotide. {ECO:0000269|PubMed:32168448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + GDP-D-glycero-alpha-D-manno-heptose = (S)-2-
CC hydroxyglutarate + GDP-D-glycero-4-keto-alpha-D-lyxo-heptose;
CC Xref=Rhea:RHEA:70211, ChEBI:CHEBI:16782, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:59971, ChEBI:CHEBI:189049;
CC Evidence={ECO:0000269|PubMed:32168448};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:32168448, ECO:0000269|PubMed:32168450};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for GDP-D-glycero-alpha-D-manno-heptose (at pH 7.4 and 30
CC degrees Celsius) {ECO:0000269|PubMed:32168448};
CC KM=130 uM for alpha-ketoglutarate (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:32168448};
CC Note=kcat is 0.64 sec(-1) with GDP-D-glycero-alpha-D-manno-heptose as
CC substrate. kcat is 0.55 sec(-1) with alpha-ketoglutarate as
CC substrate. {ECO:0000269|PubMed:32168448};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:32168448}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:32168450}.
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; AL111168; CAL35536.1; -; Genomic_DNA.
DR PIR; C81288; C81288.
DR RefSeq; WP_002858299.1; NC_002163.1.
DR RefSeq; YP_002344810.1; NC_002163.1.
DR PDB; 6VO6; X-ray; 1.50 A; A/B/C/D=1-313.
DR PDB; 6VO8; X-ray; 2.40 A; A/B=1-313.
DR PDBsum; 6VO6; -.
DR PDBsum; 6VO8; -.
DR AlphaFoldDB; Q0P8I7; -.
DR SMR; Q0P8I7; -.
DR IntAct; Q0P8I7; 5.
DR STRING; 192222.Cj1427c; -.
DR PaxDb; Q0P8I7; -.
DR PRIDE; Q0P8I7; -.
DR EnsemblBacteria; CAL35536; CAL35536; Cj1427c.
DR GeneID; 905716; -.
DR KEGG; cje:Cj1427c; -.
DR PATRIC; fig|192222.6.peg.1408; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_4_0_7; -.
DR OMA; FRRNYIH; -.
DR BioCyc; MetaCyc:MON-19062; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..313
FT /note="GDP-D-glycero-alpha-D-manno-heptose dehydrogenase"
FT /id="PRO_0000455378"
FT BINDING 13..14
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 33..39
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 37
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 57..58
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 77
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 144..148
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 168
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 169
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 175..177
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 179..184
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 196..198
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 204
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 242
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 270
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
FT BINDING 311
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000269|PubMed:32168450,
FT ECO:0007744|PDB:6VO6"
SQ SEQUENCE 313 AA; 35602 MW; D6EA9DC7429A2D66 CRC64;
MSKKVLITGG AGYIGSVLTP ILLEKGYEVC VIDNLMFDQI SLLSCFHNKN FTFINGDAMD
ENLIRQEVAK ADIIIPLAAL VGAPLCKRNP KLAKMINYEA VKMISDFASP SQIFIYPNTN
SGYGIGEKDA MCTEESPLRP ISEYGIDKVH AEQYLLDKGN CVTFRLATVF GISPRMRLDL
LVNDFTYRAY RDKFIVLFEE HFRRNYIHVR DVVKGFIHGI ENYDKMKGQA YNMGLSSANL
TKRQLAETIK KYIPDFYIHS ANIGEDPDKR DYLVSNTKLE ATGWKPDNTL EDGIKELLRA
FKMMKVNRFA NFN
