ID Q2U5I7_ASPOR Unreviewed; 742 AA.
AC Q2U5I7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=AO090113000128 {ECO:0000313|EMBL:BAE63178.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE63178.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE63178.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AP007166; BAE63178.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2U5I7; -.
DR STRING; 510516.Q2U5I7; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; BAE63178; BAE63178; AO090113000128.
DR VEuPathDB; FungiDB:AO090113000128; -.
DR HOGENOM; CLU_012773_0_0_1; -.
DR OMA; NCIHVFL; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000006564; Chromosome 5.
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.
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:UP000006564};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 711..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 84585 MW; 9C93E933E9117C26 CRC64;
MSSPYIESVL LRWTHVLAVT MMIIFTSLRG IFLPIMVVTL PLPPQLTQNY PPEFVFFLHW
FAFWTFSALL IIPWLFCVHR LVTSSIGRTQ RIKEVLDDRT APKTVIVMPV YKENPAVLIK
AINSVVDSDY PTNCIHVFLS YDGVNIDEPY LRVIHHLGIP ISLDTYPQSI DVTYREARIT
VSRFKHGGKR HCQKLTFKLI SQVYEEYNRK HDDLFMLFID SDCILDRLCL QNFMYDIELK
PGSKHNMLAM TGIITSTTEK NSLITVLQDL EYIHGQLFER SVESGCGAVT CLPGALTILR
FSAFRKMAKH YFADKAEQCE DLFDYAKCHL GEDRWLTHLF MIGAKERYQI QMCTSAFCKT
EAAQTFRTLL KQRRRWFLGY ITNEACMLTD VRLWRRYPFL CLVRLMQNTI RTTALLFFVQ
VLALMTTSSR FVDLPVGFIA ISLGLNYVLM FYFGIRLKRY KAWLYPLMFV LNPFFNWLYM
VYGIFTAGQR TWGGPRADAA KADEHTSPEE AVEQARAQGD ELNVLVDTFR AKADKKGCFN
RASEQIDRRL SGLPGHRGSH ISNHDEAMVP LASLMTSPLD VPRIGLHPNC SSDSVVTDSS
SSSISLPLDV ESLMNEEDRA KRSTALQAQE LTGILQQFAT SPDDGDIHTQ GPARLQSEGP
ETHIASEQSR GAPAFASVQK DDTVHCIPLR QPQGVLQSAY PHQSVELGVI TGNHRSLRPS
RGRRLQKTRR QASQSRDPEY MV
//
