ID A0A2G2JYT8_9PROT Unreviewed; 461 AA.
AC A0A2G2JYT8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=COA89_16830 {ECO:0000313|EMBL:PHS03482.1};
OS Acidithiobacillus sp.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1872118 {ECO:0000313|EMBL:PHS03482.1, ECO:0000313|Proteomes:UP000221235};
RN [1] {ECO:0000313|Proteomes:UP000221235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHS03482.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NVVQ01000097; PHS03482.1; -; Genomic_DNA.
DR Proteomes; UP000221235; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; 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 PANTHER; PTHR43584:SF3; BIFUNCTIONAL PROTEIN GLMU; 1.
DR PANTHER; PTHR43584; NUCLEOTIDYL TRANSFERASE; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..144
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT UNSURE 172
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:PHS03482.1"
SQ SEQUENCE 461 AA; 50294 MW; 0D38E6903FD6EA5D CRC64;
MKSWKFXXME XXDSANXIPQ QAVILAAGLG SRLQPQSDIP KPLTNMLGLT LAERVVCTLL
DVGVRRFLVT LGHEATRVRA HFSEIARRRG VTIDFIEVEG WERGNGASAL AAKGRTGEAP
FFMVMIDHLF DPXIARALAD DPPAPGEMXL AVDRDKDGIF DLDDVTRVKI DDGRITEIEK
NLXDWDAGDT GVMLCTSGLF EGLESAAATN KHSLSDGLRE LARKGRARTL DVTGMSWLDV
DTPEALXEGE RQLIHNQGRK TRDGPVSRNL NRPVSQWLSC YLVRTTVTPN QISLISWLLS
CVAAGLMAVS GYPALAAGGV LAQLASILDG CDGEIARLKH SQSEFGGWLD AVLDRYADAV
LLFGLMWHEF AATGTXLSXV LGFAAIVGSF LISYTADKYD GFMAQRLQGA SYFRXGRDVR
VFVIFLGALL NQPLFTLAVX ALVMNVEVVR RIXIXXRPPV A
//
