HDDC_CAMJE
ID HDDC_CAMJE Reviewed; 221 AA.
AC Q0P8J1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase {ECO:0000303|PubMed:31449400};
DE EC=2.7.7.71 {ECO:0000269|PubMed:31449400};
DE AltName: Full=D-alpha-D-heptose 1-phosphate guanylyltransferase {ECO:0000305};
GN Name=hddC {ECO:0000312|EMBL:CAL35532.1};
GN OrderedLocusNames=Cj1423c {ECO:0000312|EMBL:CAL35532.1};
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:CAL35532.1};
RN [1] {ECO:0000312|EMBL:CAL35532.1, 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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:31449400};
RX PubMed=31449400; DOI=10.1021/acs.biochem.9b00548;
RA Huddleston J.P., Raushel F.M.;
RT "Biosynthesis of GDP-d-glycero-alpha-d-manno-heptose for the Capsular
RT Polysaccharide of Campylobacter jejuni.";
RL Biochemistry 58:3893-3902(2019).
CC -!- FUNCTION: Catalyzes the GDP transfer from GTP to D-glycero-alpha-D-
CC manno-heptose 1-phosphate, yielding GDP-D-alpha-D-heptose. Is able to
CC use ATP, CTP or UTP as substrate in the presence of pyrophosphatase,
CC but at a significantly slower rate. Can also form GDP-alpha-D-mannose
CC from alpha-D-mannose 1-phosphate and GTP.
CC {ECO:0000269|PubMed:31449400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glycero-alpha-D-manno-heptose 1-phosphate + GTP + H(+) =
CC diphosphate + GDP-D-glycero-alpha-D-manno-heptose;
CC Xref=Rhea:RHEA:27461, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:59971, ChEBI:CHEBI:61574; EC=2.7.7.71;
CC Evidence={ECO:0000269|PubMed:31449400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=495 uM for D-glycero-alpha-D-manno-heptose 1-phosphate (at pH 7.4
CC and 25 degrees Celsius) {ECO:0000269|PubMed:31449400};
CC Note=kcat is 3.0 sec(-1) and 1.35 sec(-1) for D-glycero-alpha-D-
CC manno-heptose 1-phosphate determined by 31P NMR and HPLC method,
CC respectively. {ECO:0000269|PubMed:31449400};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-
CC heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-
CC glycero-alpha-D-manno-heptose 7-phosphate: step 3/3.
CC {ECO:0000269|PubMed:31449400}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:31449400}.
CC -!- BIOTECHNOLOGY: This enzyme is used in a preparative method to
CC synthesize ample amount of GDP-D-glycero-alpha-D-manno-heptose to be
CC used in elucidating biosynthetic pathways of various heptose components
CC present in capsular polysaccharide (CPS) of C.jejuni.
CC {ECO:0000269|PubMed:31449400}.
CC -!- SIMILARITY: Belongs to the D-alpha-D-heptose-1-P guanylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35532.1; -; Genomic_DNA.
DR PIR; G81287; G81287.
DR RefSeq; WP_002857908.1; NC_002163.1.
DR RefSeq; YP_002344806.1; NC_002163.1.
DR AlphaFoldDB; Q0P8J1; -.
DR IntAct; Q0P8J1; 3.
DR STRING; 192222.Cj1423c; -.
DR PaxDb; Q0P8J1; -.
DR PRIDE; Q0P8J1; -.
DR EnsemblBacteria; CAL35532; CAL35532; Cj1423c.
DR GeneID; 905712; -.
DR KEGG; cje:Cj1423c; -.
DR PATRIC; fig|192222.6.peg.1404; -.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_029499_2_0_7; -.
DR OMA; HRDIGNP; -.
DR UniPathway; UPA00543; UER00608.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0070568; F:guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IC:UniProtKB.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009226; P:nucleotide-sugar biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Carbohydrate metabolism; GTP-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..221
FT /note="D-glycero-alpha-D-manno-heptose 1-phosphate
FT guanylyltransferase"
FT /id="PRO_0000454935"
SQ SEQUENCE 221 AA; 25664 MW; F442ABF6F679E26E CRC64;
MQAIILCGGL GTRLKSIIKD IPKPMAPIND KPFLEFIFEY LKKQGIKEVI LAVSYKYEVI
KEYFKDEFLG IKIKYSIEKE PLGTGGAIKE TLKFVKNEAY VLNGDTFFDI DLSKLKLNES
KICLALKQMN DFDRYGTVNV DEQDLVISFE EKVFKKQGLI NGGIYLLTKD IFNDFALQEK
FSFEEFLQEN YKKLKARACI FDDYFIDIGV PEDYYHFLIN N
