ID A0A1V3N0Z3_9SPHI Unreviewed; 442 AA.
AC A0A1V3N0Z3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN ORFNames=BWD42_01220 {ECO:0000313|EMBL:OOG18623.1};
OS Sphingobacterium sp. CZ-UAM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG18623.1, ECO:0000313|Proteomes:UP000188865};
RN [1] {ECO:0000313|EMBL:OOG18623.1, ECO:0000313|Proteomes:UP000188865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG18623.1,
RC ECO:0000313|Proteomes:UP000188865};
RA Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA Zuniga C., Morales M., Revah S., Utrilla J.;
RT "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT methanotrophic consortium.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005117}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000256|ARBA:ARBA00010813}.
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:OOG18623.1}.
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DR EMBL; MTCM01000001; OOG18623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3N0Z3; -.
DR STRING; 1933868.BWD42_01220; -.
DR OrthoDB; 729130at2; -.
DR Proteomes; UP000188865; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11510:SF5; INOSITOL-3-PHOSPHATE SYNTHASE 1; 1.
DR PANTHER; PTHR11510; MYO-INOSITOL-1 PHOSPHATE SYNTHASE; 1.
DR Pfam; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..358
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
SQ SEQUENCE 442 AA; 49215 MW; 96C84A22F0ECDAC9 CRC64;
MGQQVKDANG KLGILIPGLG AVATTLIAGV ASINKGFSKP IGSVSQLSRI RLGKRTENRN
PLIKDFVPLA KLEDVVFGGW DVYEDNVYEA ASKAQVLEQG QLDAVKAELE AIQPMKAVFD
RNFVKNLDGT HIKTEKTRRE LADAVQRDIR EFKEKNGLDR VVLVWCGSTE RYIETNEAFS
TIAKLEEALD NDDQRIPPSM IYCYAAIKEG APYVNGAPNL TCDVPAIVEL AQEYGVAIAG
KDFKTGQTLM KTIVAPGLQA RALGVEGWFS TNILGNRDGL VLDDPENFKT KEVSKLSVLE
EILDAKKNPE LYGDLYHKVR INYYPPHGDN KESWDNIDIF GWLGYKMQIK INFLCRDSIL
AAPVALDLAL FIDLAQRAGM SGIQEWLSFY LKSPQTAPGL PPEHDIFKQL MKLQNTLRHI
MGEDLITHLG LDYYQELVDS IQ
//
