ID   CHS1_CANAX              Reviewed;         776 AA.
AC   P23316;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Chitin synthase 1;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
GN   Name=CHS1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=73/055;
RX   PubMed=2140148; DOI=10.1111/j.1365-2958.1990.tb00587.x;
RA   Au-Young J., Robbins P.W.;
RT   "Isolation of a chitin synthase gene (CHS1) from Candida albicans by
RT   expression in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 4:197-207(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060 / 2024;
RX   PubMed=7582026; DOI=10.1099/13500872-141-10-2673;
RA   Sudoh M., Watanabe M., Mio T., Nagahashi S., Yamada-Okabe H., Takagi M.,
RA   Arisawa M.;
RT   "Isolation of canCHS1A, a variant gene of Candida albicans chitin
RT   synthase.";
RL   Microbiology 141:2673-2679(1995).
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 (PubMed:2140148). Also
CC       involved in forming cross walls in the hyphal phase (PubMed:2140148).
CC       {ECO:0000269|PubMed:2140148}.
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   -!- ACTIVITY REGULATION: Requires proteolytic activation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Yeast and hyphal stages, the latter having a
CC       higher specific activity.
CC   -!- INDUCTION: Under certain adverse conditions.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-58 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; X52420; CAA36671.1; -; Genomic_DNA.
DR   EMBL; D43627; BAA07738.1; -; Genomic_DNA.
DR   AlphaFoldDB; P23316; -.
DR   BindingDB; P23316; -.
DR   ChEMBL; CHEMBL3480; -.
DR   VEuPathDB; FungiDB:C7_02770W_A; -.
DR   VEuPathDB; FungiDB:CAWG_05611; -.
DR   BRENDA; 2.4.1.16; 1096.
DR   PHI-base; PHI:7232; -.
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; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..776
FT                   /note="Chitin synthase 1"
FT                   /id="PRO_0000193686"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        558..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        695..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        723..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        446
FT                   /note="Missing (in Ref. 2; BAA07738)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   776 AA;  88230 MW;  DDEBC5C754DE1597 CRC64;
     MHNINNGYVP NREKTITKRK VRLVGGKAGN LVLENPVPTE LRKVLTRTES PFGEFTNMTY
     TACTSQPDTF SAEGFTLRAA KYGRETEIVI CITMYNEDEV AFARTMHGVM KNIAHLCSRH
     KSKIWGKDSW KKVQVIIVAD GRNKVQQSVL ELLTATGCYQ ENLARPYVNN SKVNAHLFEY
     TTQISIDENL KFKGDEKNLA PVQVLFCLKE SNQKKINSHR WLFNAFCPVL DPNVIVLLDV
     GTKPDNHAIY NLWKAFDRDS NVAGAAGEIK AMKGKGWINL TNPLVASQNF EYKLSNILDK
     PLESLFGYIS VLPGALSAYR YIALKNHDDG TGPLASYFKG EDLLCSHDKD KENTKANFFE
     ANMYLAEDRI LCWELVSKRN DNWVLKFVKS ATGETDVPET IAEFLSQRRR WINGAFFAAL
     YSLYHFRKIW TTDHSYARKF WLHVEEFIYQ LVSLLFSFFS LSNFYLTFYF LTGSLVSYKS
     LGKKGGFWIF TLFNYLCIGV LTSLFIVSIG NRPHASKNIF KTLIILLTIC ALYALVVGFV
     FVINTIATFG TGGTSTYVLV SIVVSLLSTY GLYTLMSILY LDPWHMLTCS VQYFLMIPSY
     TCTLQIFAFC NTHDVSWGTK GDNNPKEDLS NQYIIEKNAS GEFEAVIVDT NIDEDYLETL
     YNIRSKRSNK KVALGHSEKT PLDGDDYAKD VRTRVVLFWM IANLVFIMTM VQVYEPGDTG
     RNIYLAFILW AVAVLALVRA IGSLGYLIQT YARFFVESKS KWMKRGYTAP SHNPLN