HDDA_MYCTU
ID HDDA_MYCTU Reviewed; 386 AA.
AC O53637; F2GLR1; I6Y2T4; Q7DAG4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=D-glycero-alpha-D-manno-heptose 7-phosphate kinase {ECO:0000250|UniProtKB:Q9AGY8};
DE EC=2.7.1.168 {ECO:0000250|UniProtKB:Q9AGY8};
DE AltName: Full=D-alpha-D-heptose 7-phosphate kinase {ECO:0000303|PubMed:33412198};
DE AltName: Full=MtbHddA {ECO:0000303|PubMed:33412198};
GN Name=hddA {ECO:0000303|PubMed:33412198};
GN OrderedLocusNames=Rv0115 {ECO:0000312|EMBL:CCP42840.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ATPASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND
RP STRUCTURAL STUDIES.
RC STRAIN=H37Rv;
RX PubMed=33412198; DOI=10.1016/j.ijbiomac.2020.12.191;
RA Karan S., Behl A., Sagar A., Bandyopadhyay A., Saxena A.K.;
RT "Structural studies on Mycobacterium tuberculosis HddA enzyme using small
RT angle X-ray scattering and dynamics simulation techniques.";
RL Int. J. Biol. Macromol. 171:28-36(2021).
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 (By similarity). Exhibits ATPase
CC activity in vitro (PubMed:33412198). {ECO:0000250|UniProtKB:Q9AGY8,
CC ECO:0000269|PubMed:33412198}.
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:0000250|UniProtKB:Q9AGY8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=139.5 uM for ATP {ECO:0000269|PubMed:33412198};
CC Note=kcat is 104 min(-1) for ATPase activity.
CC {ECO:0000269|PubMed:33412198};
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:0000250|UniProtKB:Q9AGY8}.
CC -!- PATHWAY: Lipopolysaccharide biosynthesis; LPS oligosaccharide
CC biosynthesis. {ECO:0000305|PubMed:33412198}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:33412198}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP42840.1; -; Genomic_DNA.
DR RefSeq; NP_214629.1; NC_000962.3.
DR RefSeq; WP_003899819.1; NZ_NVQJ01000062.1.
DR AlphaFoldDB; O53637; -.
DR SMR; O53637; -.
DR STRING; 83332.Rv0115; -.
DR PaxDb; O53637; -.
DR DNASU; 886902; -.
DR GeneID; 886902; -.
DR KEGG; mtu:Rv0115; -.
DR PATRIC; fig|83332.111.peg.131; -.
DR TubercuList; Rv0115; -.
DR eggNOG; COG2605; Bacteria.
DR OMA; LEIHHDG; -.
DR PhylomeDB; O53637; -.
DR UniPathway; UPA00301; -.
DR UniPathway; UPA00543; UER00606.
DR Proteomes; UP000001584; Chromosome.
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:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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;
KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="D-glycero-alpha-D-manno-heptose 7-phosphate kinase"
FT /id="PRO_0000453019"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 111..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
FT SITE 11
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q9HHB6"
SQ SEQUENCE 386 AA; 40827 MW; 1269F6ECB5F40063 CRC64;
MAILRGRAPL RLGLGGGGTD VEPYSSQFGG RILSVTIDKY AYAFAERGTG DEIAFRSPDR
DRAGQASIDD LASLEEDFPL HVAVYRRVIA EFNGGTPFPL QLATQVDAPP GSGLGSSSAL
VVAMLLTTCA LIGSSPGPYE LARLAWEIER VDLGMAGGWQ DHYAAAFGGF NFMESRPNGE
VVVNPLRIRR EVIAELEASL LLYFGGVSRL SSEVIADQQR NVVERDADAL AATHSICAEA
LEMKDLLVVG DIPGFADSLL RGWQAKKRTS TRISNPAIEH AYQVAQSSGM VAGKVSGAGG
GGFLMMIVDP RRRIEVARSL ERECGGSVAP CLFTKGGAVT WHIPESTAPV RRGVADAVAS
ALGNAGILLC AGCVLATSHS TWRVPV
