ID S0EKG0_GIBF5 Unreviewed; 730 AA.
AC S0EKG0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=FFUJ_12782 {ECO:0000313|EMBL:CCT72888.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT72888.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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.
CC {ECO:0000256|ARBA:ARBA00024009}.
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 Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HF679030; CCT72888.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EKG0; -.
DR STRING; 1279085.S0EKG0; -.
DR EnsemblFungi; CCT72888; CCT72888; FFUJ_12782.
DR VEuPathDB; FungiDB:FFUJ_12782; -.
DR HOGENOM; CLU_013022_1_0_1; -.
DR OrthoDB; 2103951at2759; -.
DR Proteomes; UP000016800; Chromosome 8.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 77..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 82276 MW; 6B808CF705098A98 CRC64;
MTSLTTTPPR SILIGKQKDQ VHANVRIVHG KALSNDSDVS YTEYPVVPIP AHLADETSSN
DSYRASQPSS LRSWVFESVG TPDTQRTSVT SRPGSKGTDL IAPIPRLPIS ISNNTSVGSR
SDAGHSSTPS VDDEITPVPQ PSAERDNTPE FKSDGAEQAK PKVETASEDD VGNAVLLKRG
KRKVTIQKYV LTAGLIAVNF MFIFASWYWP RYYYIYLPFI SFPLVLNCIM IASIAAFTLI
HWVSPEEQIK PESPENMVYV IPCYNETLEE CTRSLDSLVN QTGLENHKKG IMVICDGRVR
GPGMTKTTGD YLNEDIFLHQ TQRKKIRGAY TAWDGQQMDI EISKGFYKGL PFYCIVKDQN
QGKRDSLIVI RSFLYKFNTR AQNPESIFSR EFLDSMTSWL ENEAKMDNVD HLIGMDADTV
FEDNCVTELL KESYYPNTVG VCGYVAVDFK DGNWNLWSIY QSAEYTIAQG LRRLHQSIAT
KKVSCLPGCC QLLKICDETC GDLVLIDLFG YFPKHMDGML KRIRATASED RNHICQLLVT
FPHAQTRQAL FARAYTDVPH SWNVFLSQRR RWTLGATSND LLLFCAWNTQ WWERIVAFSN
VLTWSLNVFV IASIGCMIVA FMSQPWWLIM CFAGVMIIPL LYYVIMATWL PRNLVERAQF
LLGLAVFVFL GPFLNIAVML YAVVNMDNFG WGKTRKVVTD DSEEEKSSQK DGVVSDSSST
EPKEKTATAV
//
