CHS_SAPMO
ID CHS_SAPMO Reviewed; 886 AA.
AC P48017;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Chitin synthase;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase;
GN Name=CHS;
OS Saprolegnia monoica.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=37553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mort-Bontemps F.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a major role in cell wall biogenesis.
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; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR EMBL; U19946; AAC49743.1; -; Genomic_DNA.
DR AlphaFoldDB; P48017; -.
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..886
FT /note="Chitin synthase"
FT /id="PRO_0000193714"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 98570 MW; 74E347C4B941FE0C CRC64;
MSDQLDLAAR LRALREGNAA PADPETATHT AWPAPQYHPH CRRCIHKSRS SWEGRMPRAA
PCAEAEGSYS QVPVWKDSKE TRRSYLDDEP TPQPQSLINM ANTLVQRQRR INLPAAAYSE
LPTAAQHRRG ASGRQANTAT QVLQLTCTWT LARRSSKSAE ELGTWMNTVA EEARKAALPP
QLKIARTNVP TVEQAWKGRT PPFHDADEFR LMRYTAVATK DPIQFSNDGY VLRVHQLHRR
IKVFITITMY NEEGSEILGT LTGLAKGLGY MCKEYGQDFW QEVAVAIVSD GRTKASKTCL
EYLNGLGAFD EEIMTVTSLG VDTPAGENQT FENYFPPLQV IYALKENNGG KLNSHLWFFN
AFSEQLNPKY TVLVDVGTIP AETSVFRLIR SMERNYQIGG VAGEIAVEAP NYFNPVIAAQ
HFEYKISNIM DKSLESVFGF ISVLPGAFSA YRYEAIRAVK GVGPLPEYFK SLTSTTKELG
PFQGNMYLAE DRILCFELLA RKHKQWTMHY VKDAIARTDV PETLVDLIKQ ARRWLNGSFF
AGLFAIGTLA VWSQSSHTMS RKLVFTFQFF YLALQNLLSW FLLSNLFLTF YFVLTLAFTD
SAPALLQAML TLYLAIVGGL IVFALGNKPE PRTASFYLFS CLYMGIIMML VTGISIYGLV
GKGTSAVKDP RVITGPLATV LSLKGSLSVV SSPRLGLIFL SAFVHGEFSI LLSVIQYFFM
LPTFVQFAHL SWGTKGLESG GRHGPTKTGG GKVKEVVEQQ KKLEAQRQAA AKEKEDVDNS
FRAFRSTLLA VVAHDQRHLA LRCDGLHVER VLLEGPQLVV GFFNVIVSRA ALYLLSCASL
SYSALTAVQW GPPTIPMSAT CRPTGRLITM YRTKATVGLW LPVQRA