ID C6HVQ0_9BACT Unreviewed; 179 AA.
AC C6HVQ0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=UBAL3_79520068 {ECO:0000313|EMBL:EES53347.1};
OS Leptospirillum ferrodiazotrophum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=412449 {ECO:0000313|EMBL:EES53347.1, ECO:0000313|Proteomes:UP000009374};
RN [1] {ECO:0000313|EMBL:EES53347.1, ECO:0000313|Proteomes:UP000009374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19429552; DOI=10.1128/AEM.02943-08;
RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M.,
RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J.,
RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., Banfield J.F.;
RT "Community genomic and proteomic analyses of chemoautotrophic iron-
RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum
RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.";
RL Appl. Environ. Microbiol. 75:4599-4615(2009).
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};
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DR EMBL; GG693865; EES53347.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HVQ0; -.
DR Proteomes; UP000009374; 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 Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR011914; RfaE_dom_II.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 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 SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 4: Predicted;
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:EES53347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009374};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EES53347.1}.
FT DOMAIN 43..135
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 179 AA; 19667 MW; 6B1FEDD29E59F638 CRC64;
MRDLSPPSQR PSVFSSTRTK ILDLGDLLAA LAPRREKGEK VVFTNGCFDL LHAGHIEVLE
KARQLGQILI VALNTDRSVS NLKGPNRPIV PETNRAVVMA ALECVSYVTF FDEETPRLLI
ERILPDVLVK GGDWPVERIV GSDIVLARNG TVRSIPLVPD SSTTGLIDRI LSRYSSPRG
//
