ID D5VRC1_METIM Unreviewed; 422 AA.
AC D5VRC1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Metin_0454 {ECO:0000313|EMBL:ADG13124.1};
OS Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13124.1, ECO:0000313|Proteomes:UP000002061};
RN [1] {ECO:0000313|EMBL:ADG13124.1, ECO:0000313|Proteomes:UP000002061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of Methanocaldococcus infernus ME.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002009; ADG13124.1; -; Genomic_DNA.
DR RefSeq; WP_013099870.1; NC_014122.1.
DR AlphaFoldDB; D5VRC1; -.
DR STRING; 573063.Metin_0454; -.
DR GeneID; 9131459; -.
DR KEGG; mif:Metin_0454; -.
DR eggNOG; arCOG00673; Archaea.
DR HOGENOM; CLU_643435_0_0_2; -.
DR OrthoDB; 15372at2157; -.
DR Proteomes; UP000002061; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..107
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 422 AA; 48558 MW; 65B359D8D4CB3E3F CRC64;
MDKAVILAAG LAKRMGEPET PKGLIKIAGR EILYRNMKIL ENLGVKEFII ITNTKYYKKF
EEFLKKYNFR GKVVINKEPE RENGYSLYLA KDYVKEPFIL MMSDHIYGED FLKEAIKGEG
LVADREPRYI DVEEATKVKV LNNRVKDIGK HLKEFDAVDT GFFILTPEIF KTIEKINKEK
ITLSEVMKEA EVKVHFVDGK FWTDVDTPEE IKRAKWLLIK NSVKGTGDGF ISRYINRKIS
TRISYFLVDH LTPNQMTVIS FILGILSALL CFISIPLGGI FYQISSIVDG VDGEIARASL
RTSKLGGYID SILDRYVDFF FLLVLAYLTI SSTLMWVIAC LAIFGSVMVS YSTERYKAAF
GRDIYKDIKE MKYLIGKRDE RVFLTMIFCL LQKVELLFII LAIITNIRVI LTLYLVCKKV
RE
//
