ID   HEPPA_BORBR             Reviewed;         162 AA.
AC   Q7WF17;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase;
DE            EC=2.7.7.70;
DE   AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase;
GN   OrderedLocusNames=BB4463;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, MASS SPECTROMETRY, AND
RP   PATHWAY.
RX   PubMed=20050615; DOI=10.1021/bi902018y;
RA   Wang L., Huang H., Nguyen H.H., Allen K.N., Mariano P.S.,
RA   Dunaway-Mariano D.;
RT   "Divergence of biochemical function in the HAD superfamily: D-glycero-D-
RT   manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL   Biochemistry 49:1072-1081(2010).
CC   -!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-
CC       manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
CC       Cannot use GTP, UTP, or CTP as substrate. Is not active against the
CC       alpha-anomer substrate. Is also able to catalyze the ADP transfer to
CC       beta-glucose 1-phosphate in vitro, yielding ADP-beta-glucose.
CC       {ECO:0000269|PubMed:20050615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC         D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC         Evidence={ECO:0000269|PubMed:20050615};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC       heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC       glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
CC       {ECO:0000269|PubMed:20050615}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000269|PubMed:20050615}.
CC   -!- MASS SPECTROMETRY: Mass=17322; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20050615};
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR   EMBL; BX640450; CAE34826.1; -; Genomic_DNA.
DR   RefSeq; WP_003815102.1; NC_002927.3.
DR   AlphaFoldDB; Q7WF17; -.
DR   SMR; Q7WF17; -.
DR   STRING; 257310.BB4463; -.
DR   EnsemblBacteria; CAE34826; CAE34826; BB4463.
DR   GeneID; 56477038; -.
DR   GeneID; 66440438; -.
DR   KEGG; bbr:BB4463; -.
DR   eggNOG; COG0615; Bacteria.
DR   HOGENOM; CLU_034585_2_0_4; -.
DR   OMA; KGTDYTP; -.
DR   OrthoDB; 1465613at2; -.
DR   BRENDA; 2.7.7.70; 227.
DR   UniPathway; UPA00356; UER00439.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001027; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:RHEA.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR011914; RfaE_dom_II.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR02199; rfaE_dom_II; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Lipopolysaccharide biosynthesis;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..162
FT                   /note="D-beta-D-heptose 1-phosphate adenylyltransferase"
FT                   /id="PRO_0000424238"
SQ   SEQUENCE   162 AA;  17440 MW;  CC469097A82B42EB CRC64;
     MSSARFESKI LSRAELVAAV AAGRLPRPLV FTNGVFDILH RGHVTYLDQA AQLGATLVVA
     VNTDESVRRL GKGSDRPLNQ VQDRAALLAA LGCVDAVTSF HEDTPQELIG ELRPDLIVKG
     GDYDMDTLPE TALVKSWGGR AVAIPFDFER STTALLGKIR QG