CHS1_PHYB8
ID CHS1_PHYB8 Reviewed; 841 AA.
AC P87073;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 82.
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 Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RA Miyazaki A., Ootaki T.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-370.
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX PubMed=8244024; DOI=10.1016/0378-1119(93)90186-7;
RA Miyazaki A., Momany M., Szaniszlo P.J., Jayaram M., Ootaki T.;
RT "Chitin synthase-encoding gene(s) of the Zygomycete fungus Phycomyces
RT blakesleeanus.";
RL Gene 134:129-134(1993).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB003043; BAA19857.1; -; Genomic_DNA.
DR PIR; JT0767; JT0767.
DR AlphaFoldDB; P87073; -.
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..841
FT /note="Chitin synthase 1"
FT /id="PRO_0000193708"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 179
FT /note="E -> EDE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..200
FT /note="RV -> HI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="A -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 95227 MW; 71CD6C09ACB66B8B CRC64;
MNPGQKQEHD QYPLHDTQFV PQQMDRNSPF ADPYPEDQPP PSGYDHQPLL RDNAPSYPPD
PFGQPGGYPP QSTMYPPQPM GPPSPNMRYG EAPRRQPRRY KTTRRVKLTH GNLILDCPVP
TPYLQAVPIK DTKEFTHMRY TAATCDPADF ASQGYTLRQP ILQRNTELFI VLTMYNEDEI
LFARTMHGVM KNIAHLCSRV RSNVWEGPKA WEKVVVCIVS DGRKKIHPRT LSLLATLGVY
QDGVAKNVVG DKPVTAHIYE YTTQLSVDPE MKFKGADKGM PPCQILFCLK ENNQKKINSH
RWFFQAFGPV INPNVCVLID VGTRPGKTSI YHLWKAFDIS SNIAGACGEI RAMSGTAGVA
LLNPLVAAQN FEYKMSNILD KPLESVFGYI SVLPGAFSAY RFTALQNDEN GHGPLEKYFL
GESQHGADAD IFTANMYLAE DRILCYELVA KKKANWVLHY VSSSYGETDV PDSVPEFISQ
RRRWLNGSFF AGCYALFHWR KVWASDHSFV RKLMFMFEDL YNTYNLIFSW FALGNFYLTF
YILTSALGAE SLDPKPFSAN VASILHTILN YIYILLIIVQ FILALGNRPQ GSKWAYFGSM
TFFAILMVYM MFATIWITVV GVQDAVANAD GSFTAMLGES TFRNIIISIV STYAMYFIAS
FLFFDPWHMF TSFIQYIFLS PSYTNILNIY AFCNTHDVSW GTKGDNTVST DLGVVKSKKD
GSGDTTVEVE VPTEQKDINE AYEEACVELT RQVEPEVSHR DAKTKQEDYY RSFRTRLVIS
WIISNLILVV LITNENILAS FGTFEVRSTS YLGFVLWSVA GLSAIRFCGS GLYLIFRIFM
G
