ID G0HNC9_THES4 Unreviewed; 432 AA.
AC G0HNC9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=GQS_09430 {ECO:0000313|EMBL:AEK73780.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK73780.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK73780.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK73780.1; -; Genomic_DNA.
DR RefSeq; WP_014013462.1; NC_015865.1.
DR AlphaFoldDB; G0HNC9; -.
DR STRING; 1042877.GQS_09430; -.
DR GeneID; 11016568; -.
DR KEGG; the:GQS_09430; -.
DR PATRIC; fig|1042877.9.peg.1838; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR OMA; MVSYSTE; -.
DR OrthoDB; 15372at2157; -.
DR Proteomes; UP000000874; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 261..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..114
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 432 AA; 48236 MW; A0F643DF4BC35A9B CRC64;
MVPKTAVILA AGLGKRMGER PKGLLKVAGR EILYRTLTLL RQNGVEMFII VTNERYAGFY
RKFIEEHGLN AELVVNPEPE KGNGHSLHLA KGHISGRFVL VMSDHVYGEE FIREALRGSG
LIADRKPRWA DVGEATKVKA RNGRVERIGK DLKDWDAVDT GFFVLDESIF EITEALERER
EGDYPVSEVV KMARLEVTFI DGLPWTDVDT PSDLKMARRM LIKTSVKGTG DGFVSRHLNR
KVSTEISYLL AEKATPNQMT VVTFILGMIS AFLTLFSLPL AGILYQISSI LDGVDGELAR
AQMRTSRFGG YIDSLLDRYV DGAFLALLTY STLTEPLWYL IALLALLGSV MVSYSTERFK
AAYGEDAYSS IPTLRKLPGK RDERIFLTML FLLYPVGASV KALFLLLAVL TNLRVAITAY
LISRKVLQPK TI
//