ID   HDDA_ANETH              Reviewed;         341 AA.
AC   Q9AGY8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=D-glycero-alpha-D-manno-heptose 7-phosphate kinase;
DE            EC=2.7.1.168;
DE   AltName: Full=D-alpha-D-heptose 7-phosphate kinase;
GN   Name=hddA; Synonyms=gmhB;
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, AND
RP   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 phosphorylation of D-glycero-alpha-D-manno-
CC       heptose 7-phosphate at the C-1 position to form D-glycero-alpha-D-
CC       manno-heptose 1,7-bisphosphate. {ECO:0000269|PubMed:11279237}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-alpha-D-manno-heptose 7-phosphate = ADP + D-
CC         glycero-alpha-D-manno-heptose 1,7-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:27570, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60203, ChEBI:CHEBI:60207, ChEBI:CHEBI:456216;
CC         EC=2.7.1.168; 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 1/3.
CC       {ECO:0000269|PubMed:11279237}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:11279237}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR   EMBL; AF324836; AAK27850.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AGY8; -.
DR   SMR; Q9AGY8; -.
DR   KEGG; ag:AAK27850; -.
DR   BioCyc; MetaCyc:MON-15575; -.
DR   BRENDA; 2.7.1.168; 344.
DR   UniPathway; UPA00543; UER00606.
DR   UniPathway; UPA00977; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001174; Galkinase.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR014606; Heptose_7-P_kinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF036406; Hept_kin; 1.
DR   PRINTS; PR00960; LMBPPROTEIN.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..341
FT                   /note="D-glycero-alpha-D-manno-heptose 7-phosphate kinase"
FT                   /id="PRO_0000424229"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT   SITE            10
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HHB6"
SQ   SEQUENCE   341 AA;  38102 MW;  5C65E966F958FCC5 CRC64;
     MIFRSKAPLR LGFAGGGTDV SPYSDEYGGY VLNATVDMYA YCTIEVTNDN RVCFYAADRE
     EIFEGNSLEE FELDGNLDLH KGIYNRVVKQ FNHGRPLSFR MTTYSDAPAG SGLGSSSTMV
     VAILKGFVEW LNLPLGEYDV AHLAYEIERI DVGLSGGKQD QYAATFGGFN FIEFYKEDKV
     IVNPLRIKNW IINELENSMI LYYTGVSRES AKIIDEQTKN TKEKNSRSLE AMHELKADAL
     IMKEAILKGD LKTFAEYLGK SWEAKKRMAS SISNSYLDKI YEVAIETGAY AGKVSGAGGG
     GFMMFIVDPT KKITVSRELN KMGGHTMNFH FVKHGTQGWR V