ID   CHS1_RHIOL              Reviewed;         858 AA.
AC   P30594;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 86.
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   Rhizopus oligosporus (Rhizopus microsporus var. oligosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7765484; DOI=10.1271/bbb.58.1685;
RA   Motoyama T., Sudoh M., Horiuchi H., Ohta A., Takagi M.;
RT   "Isolation and characterization of two chitin synthase genes of Rhizopus
RT   oligosporus.";
RL   Biosci. Biotechnol. Biochem. 58:1685-1693(1994).
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:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR   EMBL; D10159; BAA01023.1; -; Genomic_DNA.
DR   PIR; JC2308; JC2308.
DR   AlphaFoldDB; P30594; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
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   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..858
FT                   /note="Chitin synthase 1"
FT                   /id="PRO_0000193711"
FT   TRANSMEM        537..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        609..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..680
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        685..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        791..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  97058 MW;  EE1E6197F00E70B9 CRC64;
     MYPYNNSNNN SPMPSARLPS RPRYGGGEEY PMQQVSFNNN SPPPPPFPSS PNDTGFYDGN
     DVQRPLLVNN GSTASSVTLN NGNGGNVRFT NAKSNMIGGG PDNVGIAPRK QTRRYKTIRR
     VKLTGGNLVL DNPVPSKYLQ RVKRKDKEEF THMRYTAATC DPADFERENY KLRQNLLGRE
     TELFIVLTMY NEDEVLFCRT MNGVMKNVSH LCSRNRSSTW GPEGWKKVVV CIVSDGRTKI
     HPRTLSVLAA MGVYQEGMAK NIVEGKPVTA HIYEHTTQLS IDADMNFRGD EKGVVPVQIL
     FCLKEKNQKK INSHRWFFQA FGPLLKPNVC VLIDVGTKPG GRSIYHLWKC FDINSNVAGA
     CGEIKAMLGP GGVHLLNPLV ASQNFEYKMS NILDKPLESV FGHISVLPGA FSAYRYEALQ
     NDVNGHGPLE KYFLGEKMHG SDADIFTANM YLAEDRILCY ELVAKKGAAW VLHYCSNAYG
     ETDVPDTVAE FISQRRRWLN GSFFAGIYSM VHWSKVWSSN HNILRCIMFM FEDLYQLYNL
     IFSWFAIGNF YLVFYIMTTS INSVPNPPFA KNAGSVIHTV LNYLYVLLLI IQIIIAMGNR
     PQGYKWAYFM IIVFFAILMG YVLFCTAWIT IEGVKTAVET AQHNQDAQFI ALIKQNSFRD
     VIVSVCSTYI MYFVSSLLFL DPWHIFTSLI PYIFMSPSYI NVLNIYAFCN THDVSWGTKG
     DNGVSTDLGV VKSTKGKDGV HEVEVDLPTE QKDLNEQYEE ACMALKVAPI PEVTKRDAKT
     KQEDYYKSFR TTLVTCWIIS NLILVTIIIN GQEVWQWFGD YEKRATVYLS FILWSVAGLS
     AIRFVGSILY LFMKIFTG