ID A0A2Z5G2D4_9BACT Unreviewed; 396 AA.
AC A0A2Z5G2D4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Ceramide glucosyltransferase {ECO:0000313|EMBL:AXC13258.1};
GN ORFNames=ACPOL_3979 {ECO:0000313|EMBL:AXC13258.1};
OS Acidisarcina polymorpha.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC13258.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC13258.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC13258.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP030840; AXC13258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5G2D4; -.
DR KEGG; abas:ACPOL_3979; -.
DR OrthoDB; 9814255at2; -.
DR Proteomes; UP000253606; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR CDD; cd02520; Glucosylceramide_synthase; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AXC13258.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 396 AA; 44050 MW; 248FAC555E733E44 CRC64;
MLTFTVRDIL IGIAAIPFIY YAIALFSSIR FFLGSRAASP VGFTPPISNL KPVRGLDPDA
YENYASFCRQ DYPDYEVLFC VGDTTDPVLP VLQRLTRDFP DCKIRIVIGS GRTATNDKVA
KLARMVDEAA YEHLVISDSD VRVEPDYLRR LIAPLSDPKV GAVTCFYVPT EETSWVQRLQ
DVGMLSDFYP GILVAKQLDG VKFALGPTIA TTRARLHAFG GYSAIENQPA DDLLVGRLIA
EQGCEVVLLP YAITTVPDYQ SLSELFYKRL RWITVMRHMR PWGHLGLIFT LGLPWALMAV
AVDPTPAIAV TYLGGYFVVR AALTALVGGW GLKQKGVWKK LAWIPVWDAM ASLIWLASFA
RRTIRWRGRD YLIRNGELVP LLPAEPHANA GSEVIP
//