ID   HDDC_ANETH              Reviewed;         230 AA.
AC   Q9AGY6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase;
DE            EC=2.7.7.71;
DE   AltName: Full=D-alpha-D-heptose 1-phosphate guanylyltransferase;
GN   Name=hddC; Synonyms=gmhD;
OS   Aneurinibacillus thermoaerophilus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=143495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND PATHWAY.
RC   STRAIN=ATCC 12990 / DSM 10155 / LMG 17166;
RX   PubMed=11279237; DOI=10.1074/jbc.m100378200;
RA   Kneidinger B., Graninger M., Puchberger M., Kosma P., Messner P.;
RT   "Biosynthesis of nucleotide-activated D-glycero-D-manno-heptose.";
RL   J. Biol. Chem. 276:20935-20944(2001).
CC   -!- FUNCTION: Catalyzes the GDP transfer from GTP to D-glycero-alpha-D-
CC       manno-heptose 1-phosphate, yielding GDP-D-alpha-D-heptose. Cannot use
CC       ATP, CTP, dTTP or UTP as substrate. {ECO:0000269|PubMed:11279237}.
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:11279237};
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:11279237}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:11279237}.
CC   -!- SIMILARITY: Belongs to the D-alpha-D-heptose-1-P guanylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AF324836; AAK27852.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AGY6; -.
DR   SMR; Q9AGY6; -.
DR   KEGG; ag:AAK27852; -.
DR   BioCyc; MetaCyc:MON-15576; -.
DR   BRENDA; 2.7.7.71; 344.
DR   UniPathway; UPA00543; UER00608.
DR   UniPathway; UPA00977; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
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   Carbohydrate metabolism; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..230
FT                   /note="D-glycero-alpha-D-manno-heptose 1-phosphate
FT                   guanylyltransferase"
FT                   /id="PRO_0000424230"
SQ   SEQUENCE   230 AA;  26623 MW;  57C688F721765A90 CRC64;
     MEAIILVGGL GKRLRSVVSE LPKPMAPIDN KPFLHYIFWY LNKQGIDQVI LSTGYKHEMI
     ETYFGNRYHG ISINYSIEQE PLGTGGAIKK AFRKTTEENV VIINGDTLFL VDLRKMFERH
     ISFKADLTLA LKPMKEFERY GTVITRDSRV IAFKEKGYHS EGNINGGVYI ANKAIFECES
     LSEKFSFEQD FLEKEFLQKK FYGFISDAYF IDIGIPDDYR KAQKELQHYI