ID S0EBT6_GIBF5 Unreviewed; 767 AA.
AC S0EBT6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=FFUJ_12279 {ECO:0000313|EMBL:CCT72411.1};
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:CCT72411.1, 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; CCT72411.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EBT6; -.
DR STRING; 1279085.S0EBT6; -.
DR EnsemblFungi; CCT72411; CCT72411; FFUJ_12279.
DR VEuPathDB; FungiDB:FFUJ_12279; -.
DR HOGENOM; CLU_012773_1_0_1; -.
DR OrthoDB; 2784803at2759; -.
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:SF41; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 570..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 88134 MW; 7DB5546713C3373A CRC64;
MALLKDWPLQ NVIYTSIVGI VLLMACLEWF LWLAAFVYCL VKVFQKAEHW SINVLCIIVG
TVFVLLRVIF LPIMVVTLPL PDTVTKLWPK EMVSFLQWFA FWAFAILLTV PWLFCIYQVV
TNQLGRTKRM KQVLDDVTAP KVVIVMPCYR EEPEVLLKAV KSVVECDYPP ACIHVFLSFD
GVEEDELYLS TIDKLGVSMK METYPTSIDV TYRSARVTIS RFEHGGKRHC QKVTFKLIDR
VYEEYLKRND NLFILFIDSD CILDKVCLQN FIYDMELSPG NSRDMLAMTG VITSTTKKHS
IITLLQDMEY IHGQLFERTV ESGCGSVTCL PGALTMLRFS AFRRMAKYYF VDKTEHCEDL
FDFAKCHLGE DRWLTHLFMI GARKRYQIQM CTSAFCKTEA VQTYRSLVKQ RRRWFLGFIT
NEVCMLTDWR LWKRYPVLIL VRFMQNTIRT TALLFFIMVL ALITTVKKVD DLPVGFIAVS
LGLNWLLMLY FGAKLRRFKI WLYPLMFILN PFYNWLYMVY GIFTAGQRTW GGPRADAAAA
DAHTTAREAV EQAEKQGDEL NVVPETFKAA HEARRAPSNR KSTATTELGR TRSVVRPPDK
IDGKFSARQK TASGTYAHPD EIDTSTEDIE MGKATSHVFS KPQECADLEV GTQGRMKLLM
DEENIRKYEI AQQIQDRASQ VRDLEGIQSS HGFSASSMRR AEISGDMTTS RSPIEYNQVA
QDEPVESRCR NSTERSIGTS LEGEQTRLGS NMSFASRMTR GRLKKSR
//
