ID C1DHT3_AZOVD Unreviewed; 851 AA.
AC C1DHT3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Glucans biosynthesis glucosyltransferase H {ECO:0000256|ARBA:ARBA00020585, ECO:0000256|HAMAP-Rule:MF_01072};
DE EC=2.4.1.- {ECO:0000256|HAMAP-Rule:MF_01072};
GN Name=mdoH1 {ECO:0000313|EMBL:ACO80666.1};
GN Synonyms=opgH {ECO:0000256|HAMAP-Rule:MF_01072};
GN OrderedLocusNames=Avin_45520 {ECO:0000313|EMBL:ACO80666.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO80666.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO80666.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
CC -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC glucans (OPGs). {ECO:0000256|HAMAP-Rule:MF_01072}.
CC -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005001, ECO:0000256|HAMAP-
CC Rule:MF_01072}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01072}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01072}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. OpgH
CC subfamily. {ECO:0000256|ARBA:ARBA00009337, ECO:0000256|HAMAP-
CC Rule:MF_01072}.
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; CP001157; ACO80666.1; -; Genomic_DNA.
DR RefSeq; WP_012703033.1; NC_012560.1.
DR AlphaFoldDB; C1DHT3; -.
DR STRING; 322710.Avin_45520; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; ACO80666; ACO80666; Avin_45520.
DR KEGG; avn:Avin_45520; -.
DR eggNOG; COG2943; Bacteria.
DR HOGENOM; CLU_015730_0_0_6; -.
DR OrthoDB; 9775281at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04191; Glucan_BSP_MdoH; 1.
DR HAMAP; MF_01072; MdoH_OpgH; 1.
DR InterPro; IPR023725; Glucans_biosynth_gluTrFase_H.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR PANTHER; PTHR43867:SF5; GLUCANS BIOSYNTHESIS GLUCOSYLTRANSFERASE H; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_01072}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01072};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01072};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01072};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01072};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01072};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01072}.
FT TRANSMEM 136..153
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 185..214
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 509..537
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 564..588
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 600..621
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT TRANSMEM 677..703
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01072"
FT DOMAIN 243..425
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 851 AA; 95568 MW; A01140F49B62D663 CRC64;
MNNPTPPETP LAEYLEHLPL DALERERLAD ADSLAELHRR LAGASPAPAG DPALASAARR
LGLGDRERDG IDMDDAGRPC LKAAPPIRRT KVVPEPWRTN VLVRLWYRLT GRRSPPRPTR
DLPKARWRRV GSLRRLILLV LMLGQTALAT WYMKGILPYQ GWAFVDLAEI SRQSWQQSLQ
QVLPYILQFG VLFLFTILFC WVSAGFWTAL MGFWELLSGR DRYRISGSSA GDEPIAAEAR
TAIVMPICNE DVARVFAGLR ATYESLAATG ELARFDFFVL SDSSSADIAV AEQQAWLEVC
RETGGSGRIF YRRRRRRVKR KSGNIDDFCR RWGSQYRYMV VMDADSVMSG DCLAKLVRLM
EANPEAGIIQ TAPKASGMDT LYARLQQFAT SVYGPLFTAG LHFWQLGESH YWGHNAIIRV
KPFIEHCALA PLSGRGAFAG AILSHDFVEA ALMRRAGWGV WIAYDLPGSY EELPPNLLDE
LKRDRRWCHG NLMNFRLFLV KGMHPVHRAV FLTGVMSYLS APLWFAFLVL STALLAVHQL
MEPQYFLAPR QLFPIWPQWH PERAIALFST TLTLLFLPKL LSVILVWAKG AKAYGGAFKV
ALSMLLEMLF SMLVAPVRML FHTRFVIAAF LGWSVQWKSP QRDDDATTWG EAVRRHGGQT
LLGIAWALLV AWLNPRFLWW LSPILGSLIL SIPVSVVTSW VGWGLRARRG RLFLIPEEYD
TPPELRATER YTGENRQRAF GDGFIRAAVD PWLNALACAM GTARHGTAEA IERRRRERVE
QALAAGPEGL DGESRLALLS DPVALARLHL RLWEEGRENW LAPWRQPLAG ACRSGVAAGS
TPEAAGLLLA R
//
