ID A0A7V1DIS6_9BACT Unreviewed; 351 AA. AC A0A7V1DIS6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 28-JUN-2023, entry version 9. 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 Name=rfaE2 {ECO:0000313|EMBL:HEA83789.1}; GN ORFNames=ENI03_00705 {ECO:0000313|EMBL:HEA83789.1}; OS Thermodesulfobacterium geofontis. OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria; OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; OC Thermodesulfobacterium. OX NCBI_TaxID=1295609 {ECO:0000313|EMBL:HEA83789.1}; RN [1] {ECO:0000313|EMBL:HEA83789.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HyVt-36 {ECO:0000313|EMBL:HEA83789.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-e00719(2020). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HEA83789.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DRHB01000028; HEA83789.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7V1DIS6; -. DR Proteomes; UP000885696; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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 GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR011914; RfaE_dom_II. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR43793:SF2; BIFUNCTIONAL PROTEIN HLDE; 1. DR PANTHER; PTHR43793; FAD SYNTHASE; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR02199; rfaE_dom_II; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000313|EMBL:HEA83789.1}; KW Transferase {ECO:0000313|EMBL:HEA83789.1}. FT DOMAIN 1..176 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:HEA83789.1" SQ SEQUENCE 351 AA; 39495 MW; 5644F3C92D78C636 CRC64; ESINEALLEV QKLTKSYGKS VLLGAPHYEK NEIYNAIYFI SPQSIEVLAE KNLLFPELDK SFSSGKKRKF LEISGLKVGI IICFELRSPE VARTLTKEGM DLLAVFAQWP KARIQHWEAL LRARAIENQI FVVGVNALSQ IENLVIAGHS LSFSPSGDAL NKKSEKEEII EISLPLKLEK LPYPMKTPCL KISHKIKSLD ELKSIIQKRK EKGQVMVFTN GCFDILHAGH IHYLNSARAL GDFLVVGLNS DKSVKKIKGA LRPINSEKER AYALAGLECV DYVIFFDEET PERLIKALKP DVLVKGADWE ENKIVGASFV KSYGGKVERI SFEFDTSTTK IIEKILKIYK D //