CHS1_EXODE
ID CHS1_EXODE Reviewed; 988 AA.
AC P30600; O74681;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-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;
DE AltName: Full=Class-II chitin synthase 1;
GN Name=CHS1;
OS Exophiala dermatitidis (Black yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=5970;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8656;
RA Zheng L., Mendoza A.L., Wang Z., Szaniszlo P.J.;
RT "Characterization of WdCHS1, a class II chitin synthase gene, and multiple
RT wdchs mutants of Wangiella dermatitidis.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-468.
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).
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. Class II subfamily.
CC {ECO:0000305}.
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DR EMBL; AF054503; AAC36064.1; -; Genomic_DNA.
DR EMBL; M81905; AAA30334.1; -; Genomic_DNA.
DR PIR; E45189; E45189.
DR AlphaFoldDB; P30600; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR VEuPathDB; FungiDB:HMPREF1120_07981; -.
DR BRENDA; 2.4.1.16; 6682.
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 GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR001173; Glyco_trans_2-like.
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 Pfam; PF13632; Glyco_trans_2_3; 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..988
FT /note="Chitin synthase 1"
FT /id="PRO_0000193694"
FT TRANSMEM 577..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 29..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 265..266
FT /note="CV -> KL (in Ref. 2; AAA30334)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="I -> L (in Ref. 2; AAA30334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 111221 MW; 5940234B344F88A4 CRC64;
MVPFWTVVTD QHIKYTSHNK AGFIIDEEQH HWPPSSGSSL GRAPSIPLSS SNPRSPIRPS
TPSRVSTDWT RPPAPSVAYE ARDINGSPRL EPHHHNMEEV LEGLCHRAAL FGQGGCGRND
NPNARAGVGK RCLCRSLLDN AGQRPKGKLE IGTFVHDCLD LYGRWCHYQS EVESLWPSAG
RKTRYARPSR STNDQEGGYV DQWRADSRMY IPTILHSFLP RRDEREFTHM RYTAVTCDPD
DFVVKGYKLR QNIGPTMRET ELFICVTMYN EDEIEFTRTM HGIMRNIAHF CSRTRSRTWG
KDGWQKIVVC VIADGRQKVH PRTLNALAAM GVYQDGIAKN VVNQKEVTAH VYEYTTQVSL
DETLKFKGAE KGIVPCQMIF CLKEKNKKKL NSHRWFFNAF GRALIPNVCI LLDVGTKPDS
KALYHLWKAF DQNSNVAGAA GEIKADKGKG WLGLLNPLVA SQNFEYKISN ILDKPLESVF
GYITVLPGAL SAYRYHALQN DPSGHGPLSQ YFKGETLHGR DADVFTANMY LAEDRILCWE
LVAKRDEQWV LKFVKSAYGE TDVPDTVPEF ISQRRRWLNG AFFAAVYALV HFKQIWRTDH
SLTRKILLHI EFIYQFISLL FTFFSLANFY LTFYFVAGSL ADPTIDPFGH NIGKYIFVIL
RYVCVLLICL QFILSLGNRP QGEEIVSEYH GDVFHHHGIH DLCLRVYCHQ ATYDARSRKD
RPQQSYKLGN NIFTNLIVSS VSTIGLFFLM SFLYLDPWHM FTSSAQYFAL LPSYICTLQV
YAFCNTHDVT WGTKGDNVMH TDLGAAKAIG SGNTVEVEMP SEQLDIDSAY DVALRNLRDR
VEVPKPPVSE NQLQEDYYKS VRTYVVASYM VCNAILAMAV SEAYPVGSHI GSNFYLTFIL
WSVAALALFR AIGSSAFGVI NIVSAIAEGR IQAKFERIFG GGDERGRHRA GLGSGFSESG
KTGITSGSGM SGMSLSDVTS KISEKLAG
