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Database: UniProt
Entry: B5YI06_THEYD
LinkDB: B5YI06_THEYD
Original site: B5YI06_THEYD 
ID   B5YI06_THEYD            Unreviewed;       332 AA.
AC   B5YI06;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012519};
DE            EC=2.7.7.70 {ECO:0000256|ARBA:ARBA00012519};
GN   OrderedLocusNames=THEYE_A0223 {ECO:0000313|EMBL:ACI21022.1};
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21022.1, ECO:0000313|Proteomes:UP000000718};
RN   [1] {ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI21022.1, ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RX   PubMed=25635016;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT   Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL   Genome Announc. 3:0-0(2015).
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:0000256|ARBA:ARBA00000534};
CC   -!- SIMILARITY: Belongs to the KdsC family.
CC       {ECO:0000256|ARBA:ARBA00005893}.
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DR   EMBL; CP001147; ACI21022.1; -; Genomic_DNA.
DR   RefSeq; WP_012545750.1; NC_011296.1.
DR   RefSeq; YP_002248072.1; NC_011296.1.
DR   AlphaFoldDB; B5YI06; -.
DR   STRING; 289376.THEYE_A0223; -.
DR   EnsemblBacteria; ACI21022; ACI21022; THEYE_A0223.
DR   KEGG; tye:THEYE_A0223; -.
DR   PATRIC; fig|289376.4.peg.220; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG1778; Bacteria.
DR   HOGENOM; CLU_836615_0_0_0; -.
DR   InParanoid; B5YI06; -.
DR   OrthoDB; 9805604at2; -.
DR   Proteomes; UP000000718; 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:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd01630; HAD_KDO-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR010023; KdsC_fam.
DR   InterPro; IPR011914; RfaE_dom_II.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR   NCBIfam; TIGR01670; KdsC-phosphatas; 1.
DR   NCBIfam; TIGR02199; rfaE_dom_II; 1.
DR   PANTHER; PTHR43793:SF2; BIFUNCTIONAL PROTEIN HLDE; 1.
DR   PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SFLD; SFLDG01138; C1.6.2:_Deoxy-d-mannose-octulo; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:ACI21022.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACI21022.1}.
FT   DOMAIN          26..147
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   332 AA;  37503 MW;  80DCB0B325D2A858 CRC64;
     MGKIVHAMKL KNEIDNLKKQ GNKIVFTNGC FDIIHVGHVR YLKEAKKLGD ILVIGLNSDK
     SVKKIKPLRP INPENERAEV LSSLEMVDFV TFFDEETPYN LIKFLEPDVL VKGGDWKVEN
     IVGAELVKEV HSLPYIEGIS TTGIIERILK NYTTKNLSDE IIKKAKNIKF LILDVDGVLT
     SGGIILDNEN NELKIFNVRD GHGLVMLHKS GINLAVITGR HSKALERRMK ELGIAEVYQG
     TREKLKIFNE IVEKYNLKKE EIAAMGDDII DLSILDRVGL SVCPQDAHEE VKKRVNYVTE
     QKAGQGAVRE LCDIILKAKG LWDKFVDEYK NL
//
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