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Database: UniProt
Entry: G0HNC9_THES4
LinkDB: G0HNC9_THES4
Original site: G0HNC9_THES4 
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
//
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