CHS6_USTMA
ID CHS6_USTMA Reviewed; 1180 AA.
AC O13395; A0A0D1CR95; Q4PA11;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Chitin synthase 6;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 6;
DE AltName: Full=Class-V chitin synthase 6;
GN Name=CHS6; ORFNames=UMAG_10367;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=518;
RX PubMed=9454647; DOI=10.1006/fgbi.1997.1014;
RA Xoconostle-Cazares B., Specht C.A., Robbins P.W., Liu Y., Leon C.,
RA Ruiz-Herrera J.;
RT "Umchs5, a gene coding for a class IV chitin synthase in Ustilago maydis.";
RL Fungal Genet. Biol. 22:199-208(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17042749; DOI=10.1111/j.1567-1364.2006.00133.x;
RA Ruiz-Herrera J., Xoconostle-Cazares B., Reynaga-Pena C.G., Leon-Ramirez C.,
RA Carabez-Trejo A.;
RT "Immunolocalization of chitin synthases in the phytopathogenic dimorphic
RT fungus Ustilago maydis.";
RL FEMS Yeast Res. 6:999-1009(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16314447; DOI=10.1105/tpc.105.037341;
RA Weber I., Assmann D., Thines E., Steinberg G.;
RT "Polar localizing class V myosin chitin synthases are essential during
RT early plant infection in the plant pathogenic fungus Ustilago maydis.";
RL Plant Cell 18:225-242(2006).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000269|PubMed:16314447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16314447};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17042749}; Multi-pass membrane protein
CC {ECO:0000255}. Note=A constitutive cytoplasmic pool is present that
CC localizes to intracellular microvesicles termed chitosomes. Chitosomes
CC constitute a separate secretory route distinct from the typical
CC secretory pathway and serve as a vehicle for delivering the enzyme to
CC the sites on the cell surface where polysaccharide sythesis takes
CC place. Localizes to septa of yeast-like cells and to the basal septum
CC separating the living tip cell from the vacuolated part in hyphae. Also
CC localizes to the growing bud tip in yeast-like cells and in a tip-ward
CC gradient at the hyphal apex. {ECO:0000269|PubMed:16314447,
CC ECO:0000269|PubMed:17042749}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class V subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84285.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF030554; AAB84285.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CM003146; KIS69073.1; -; Genomic_DNA.
DR PIR; T42022; T42022.
DR RefSeq; XP_011389509.1; XM_011391207.1.
DR AlphaFoldDB; O13395; -.
DR STRING; 5270.UM03052P0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; O13395; -.
DR EnsemblFungi; KIS69073; KIS69073; UMAG_10367.
DR GeneID; 23566410; -.
DR KEGG; uma:UMAG_10367; -.
DR VEuPathDB; FungiDB:UMAG_10367; -.
DR eggNOG; KOG2571; Eukaryota.
DR InParanoid; O13395; -.
DR OrthoDB; 134286at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1116; -.
DR PHI-base; PHI:389; -.
DR Proteomes; UP000000561; Chromosome 7.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 2.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF00173; Cyt-b5; 2.
DR Pfam; PF08766; DEK_C; 1.
DR SMART; SM01117; Cyt-b5; 2.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS51998; DEK_C; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Cytoplasmic vesicle;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1180
FT /note="Chitin synthase 6"
FT /id="PRO_0000193724"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1118..1175
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 196
FT /note="G -> R (in Ref. 1; AAB84285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1180 AA; 130623 MW; 72974D483D5F684B CRC64;
MSTKDAHDPF ATPLETITHD PLAETAGLKA DYDKRAYGEA NPALMGTLEK DDMANRPIDA
VEEVPTTSIR KWWVRLTWFT TWWIPSFVLS KCGGMKRPDV QMAWREKFTI CAIIFWLCAI
ILFYIIAFGR LLCPDYDKAW NLSQLSQHAG ENDYYAAVRG TVYDFSKFYK GDHSDITNLQ
TSSDLMLQLA GQDLTGYFPV PLSVGCQSLV SDTSLALMPT ANNTPLISQA IHTSGPLQGD
TSSKLHDINW YPDRFLPFVK KLRKGYYVYS KKDLANQGQW RNWAVIHGKV YDLSNYLNTV
STYQTNPAYS FLDSSIVSLF KSQAGSDITA DFEDAMSTFN QTYRGATQAC LDNVFYVGRT
DFRDTARCEV QNYLLLAFSV LLVTTVLAKF IAALQLGTKR SPEQQDKFVI CQVPCYTEGE
EELRKTIDSL AGLEYDDKRK LLFLICDGMI VGSGNDRSTP RIVLDILGVD PKIDPEPLMF
KSVAEGSKQL NYAKVYSGLY EFEGHVVPYI VVVKVGRPSE RSRPGNRGKR DSQILLMRYL
NRVHFDAPMF PLELEIYHQM KNVIGIDPAF YEYILMVDAD TRVEADGLNR LVANCADDSS
IIAICGETTL DNAEGSWWTM IQVYEYYISH HLSKAFESLF GSVTCLPGCF SLYRIRSSDK
GRPLFISNRI IDDYSENRVD TLHKKNLLHL GEDRYLTTLV LKNFPSFRTK FVPDAKALTS
APDRFGVLLS QRRRWINSTV HNLAELVLMP ELCGFCLFSM RFIVFIDLLG TVILPATAVY
LVYLIVTVAT KSAPIPYISI AMIAAVYGLQ AILFLLKRQW QYIGWLVIYI LAYPVFSFFL
PIYSFWHMDD FSWGNTRIVV GEKGNKKIVA GTDDEPYDDT MIPLKRFSEY QREVWEEEAA
APSMRSGMTG ASGPFGNSQA ILHSGPPSVY RAGGSAYAGS VAGSDYGAGL GDYYQNTNVL
QKPAHSRQTS AAALSQMGGS QAASMMFGTG TPSVYGMAGM GSMYGMPGSS ASMYGLPNPM
MNTTASMYGL PPMLANPLGA NHSPAHSDIG VSMPVSQQNT GGSHIWAQPP EAATVAANSG
RGSGMQARPV STLSALNATN PFGVTAVARA LAVNEASDPT DEEIKSAVQT YLANQPSLMN
VTKRSVREAL VAAFPNAELS YKKSMINKAI DDTLSGGAQA
