ID D2RHQ4_ARCPA Unreviewed; 424 AA.
AC D2RHQ4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Bifunctional IPC transferase and DIPP synthase {ECO:0000256|ARBA:ARBA00018322};
DE EC=2.7.7.74 {ECO:0000256|ARBA:ARBA00012504};
DE EC=2.7.8.34 {ECO:0000256|ARBA:ARBA00013268};
GN OrderedLocusNames=Arcpr_0766 {ECO:0000313|EMBL:ADB57829.1};
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB57829.1, ECO:0000313|Proteomes:UP000001901};
RN [1] {ECO:0000313|EMBL:ADB57829.1, ECO:0000313|Proteomes:UP000001901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC {ECO:0000313|Proteomes:UP000001901};
RX PubMed=21304717;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + CDP-1L-myo-inositol = bis(1L-
CC myo-inositol) 3,1'-phosphate 1-phosphate + CMP + H(+);
CC Xref=Rhea:RHEA:31327, ChEBI:CHEBI:15378, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:62573, ChEBI:CHEBI:62576; EC=2.7.8.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3-phosphate + CTP + H(+) = CDP-1L-myo-inositol
CC + diphosphate; Xref=Rhea:RHEA:30647, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58401,
CC ChEBI:CHEBI:62573; EC=2.7.7.74;
CC Evidence={ECO:0000256|ARBA:ARBA00000729};
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|RuleBase:RU003750}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CDP-alcohol
CC phosphatidyltransferase class-I family.
CC {ECO:0000256|ARBA:ARBA00006982}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MobA family.
CC {ECO:0000256|ARBA:ARBA00007897}.
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DR EMBL; CP001857; ADB57829.1; -; Genomic_DNA.
DR RefSeq; WP_012940165.1; NC_013741.1.
DR AlphaFoldDB; D2RHQ4; -.
DR STRING; 572546.Arcpr_0766; -.
DR PaxDb; 572546-Arcpr_0766; -.
DR GeneID; 8739426; -.
DR KEGG; apo:Arcpr_0766; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR OrthoDB; 15372at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProt.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; NF041135; IPPtranDIPPsyn_Thcocales; 1.
DR PANTHER; PTHR19136:SF84; BIFUNCTIONAL IPC TRANSFERASE AND DIPP SYNTHASE; 1.
DR PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001901};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 256..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..110
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 424 AA; 48923 MW; 97EC1D31BB807B7E CRC64;
MKAVVLCAGF GTRMGRTVKP LLKVAGREIM FRNLKLLQDN GIDEFVVVVN NENRKAIEDF
LKRNNFKYRI VVNPHPERGN GYSFYLAKDF VDDRFVLVMG DHVYDEEFVR VALRGDGLIC
DRNPLYVDID EATKVLVENG RIKRIGKDLK EWCCVDTGFF ILTRDVFKYA EEIIDREEIK
LSDIIERSRI KVTEISGLFW MDVDTPEELK KANKLLVRKS YKGRGDGFVS RRINRKISLR
LSELLVNRIT PNQATLISFL VGIFSAILNL FSIPLAGLVY QISSILDGID GEIARASLRT
SKFGGWLDSV LDRYVDFLFL LTLSFVSNLN NLEWIIACFA MFGSFMVSYT TERYKGAFFS
DFYNDFDFKF PGKRDERIFL IFLFCLFSFL GKFVIVTLLA LIAVITNLRV VTTIYIVYKN
KRFV
//
