ID   CHS1_USTMA              Reviewed;         919 AA.
AC   P30598; A0A0D1DR09; Q4P2M6;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 3.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Chitin synthase 1;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
GN   Name=CHS1; ORFNames=UMAG_10718;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-435.
RX   PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA   Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA   Robbins P.W.;
RT   "Classification of fungal chitin synthases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
RN   [4]
RP   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. {ECO:0000305}.
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:0000269|PubMed:16314447}. Cytoplasmic
CC       vesicle membrane {ECO:0000269|PubMed:16314447}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:16314447}. Note=A constitutive cytoplasmic
CC       pool is present that localizes to intracellular microvesicles termed
CC       chitosomes. Chitosomes constitute a separate secretory route distinct
CC       from the typical secretory pathway and serve as a vehicle for
CC       delivering the enzyme to the sites on the cell surface where
CC       polysaccharide sythesis takes place (By similarity). Localizes to septa
CC       of yeast-like cells and to the basal septum separating the living tip
CC       cell from the vacuolated part in hyphae. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class III subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CM003155; KIS66849.1; -; Genomic_DNA.
DR   EMBL; M82958; AAA34224.1; -; Genomic_DNA.
DR   PIR; F45189; F45189.
DR   RefSeq; XP_011391524.1; XM_011393222.1.
DR   AlphaFoldDB; P30598; -.
DR   STRING; 5270.UM05637P0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; KIS66849; KIS66849; UMAG_10718.
DR   GeneID; 23566709; -.
DR   KEGG; uma:UMAG_10718; -.
DR   VEuPathDB; FungiDB:UMAG_10718; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   InParanoid; P30598; -.
DR   OrthoDB; 256142at2759; -.
DR   BRENDA; 2.4.1.16; 6587.
DR   PHI-base; PHI:1115; -.
DR   Proteomes; UP000000561; Chromosome 16.
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   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 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..919
FT                   /note="Chitin synthase 1"
FT                   /id="PRO_0000193721"
FT   TRANSMEM        594..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        630..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        668..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        742..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        843..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        887..919
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        292
FT                   /note="K -> E (in Ref. 3; AAA34224)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   919 AA;  103669 MW;  80DD439C849C42CB CRC64;
     MSYDAYQMRP GQGRDYARQQ RQQRSYQLSD DPLRQPGAPY ANPAGGYPSS ASMNPENPFY
     AAENPSFQTL APATSEGHAT YTYEEDKIPL TDSADEKYGF SQNGHSTYNL ASQSGFPPST
     PCGGPSSYSS ALGPEDSASQ VAWAKRQQAP KRGLTKKIQL TRGHWIVDHP VPTAVKNSVE
     SRWSQGNRTQ EFTHMRYTAA TCDPDEFTLE NGWSLRTSQQ YGRDTELLIA ITYYNEDRIL
     LARTLHGVML NIRDICKSKS SKFWRRSAEE GRPGWQRIVV SLIFDGIDPC DKEVLDLLAT
     VGVYQDGVMK RKVDGKDTVA HLFEYTTQLS VDPTPALIQP HADDASNLVP VQMIFCLKQK
     NSKKINSHRW LFNALGRHLQ PELCVLIDAG TKPGHKSLYY LWEAFYNNAN LGGACGEIHA
     MIKNGRKLIN PLVAAQNFEY KMSNILDKPL ESTFGYVSVL PGAFSAYRFR AIQGRPLQQY
     FHGDHTLADR LGKKGLHGMD IFTKNMFLAE DRILCFELVA KAGDKWTLTY VKPSKGETDV
     PEGAAELISQ RRRWLNGSFA ASIYSLVHFF RIYKSNHGII RLFFLHIQAL YNAIVLLFSW
     FALANLWLTF SIIIEFLPDE LLKNSSHTTL VVFHWINQAA KWIYVFFLVL QFVLALGNRP
     KGEKPTYIAS FIVFGILGLY LIFVSLWLTL KALLETSVSG NIWHTLFNQT TGVLIAALAA
     TFGIYLIASI LYADPWHMVT SFPQYMMIAP SFINILNVYA FCNLHDVSWG TKGSDKADAL
     PTVDTKKDKS TEPGTVEEIE RHQDDIDETF KAVVSRAVAP FKPAETVEKP TMDDSNKTFR
     TRLVAFWLLT NGALTVAIEN VNGLNTGLTN KQIEQQQSSK QSTYFRIILW ATFGLSAFRF
     IGCLIYWVKR NSTRCFRKT