CHSG_ASPFU
ID CHSG_ASPFU Reviewed; 911 AA.
AC P54267; Q09031; Q09032; Q4WYV7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Chitin synthase G;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase G;
DE AltName: Full=Class-III chitin synthase G;
GN Name=chsG; ORFNames=AFUA_3G14420;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H237;
RX PubMed=8736545; DOI=10.1046/j.1365-2958.1996.5571084.x;
RA Mellado E., Aufauvre-Brown A., Gow N.A.R., Holden D.W.;
RT "The Aspergillus fumigatus chsC and chsG genes encode class III chitin
RT synthases with different functions.";
RL Mol. Microbiol. 20:667-679(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=SIU001;
RX PubMed=8953267; DOI=10.1006/fgbi.1996.0035;
RA Borgia P.T., Iartchouk N., Riggle P.J., Winter K.R., Koltin Y.,
RA Bulawa C.E.;
RT "The chsB gene of Aspergillus nidulans is necessary for normal hyphal
RT growth and development.";
RL Fungal Genet. Biol. 20:193-203(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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:0000269|PubMed:8953267}.
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. Class III subfamily.
CC {ECO:0000305}.
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DR EMBL; X94244; CAA63928.1; -; Genomic_DNA.
DR EMBL; U39478; AAB07678.1; -; Genomic_DNA.
DR EMBL; U39479; AAB07679.1; -; mRNA.
DR EMBL; AAHF01000002; EAL92146.1; -; Genomic_DNA.
DR PIR; JC6016; JC6016.
DR RefSeq; XP_754184.1; XM_749091.1.
DR AlphaFoldDB; P54267; -.
DR STRING; 746128.CADAFUBP00003405; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; EAL92146; EAL92146; AFUA_3G14420.
DR GeneID; 3511996; -.
DR KEGG; afm:AFUA_3G14420; -.
DR VEuPathDB; FungiDB:Afu3g14420; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_0_1_1; -.
DR InParanoid; P54267; -.
DR OMA; FWIFSNA; -.
DR OrthoDB; 256142at2759; -.
DR PHI-base; PHI:3044; -.
DR PHI-base; PHI:565; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0030448; P:hyphal growth; IMP:AspGD.
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 2: Evidence at transcript level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..911
FT /note="Chitin synthase G"
FT /id="PRO_0000193682"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 879..899
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 334..337
FT /note="PPVQ -> LPSK (in Ref. 1; CAA63928)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="R -> C (in Ref. 2; AAB07679)"
FT /evidence="ECO:0000305"
FT CONFLICT 628..629
FT /note="IV -> MM (in Ref. 2; AAB07679)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="F -> N (in Ref. 2; AAB07679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 101670 MW; BC893F8BA00BE48D CRC64;
MAYQGSGSHS PPHYDDNGHR LQDLPHGSYE EEASRGLLSH QQGPFTGPFD DPQQHGSSTT
RPVSGYSLSE TYAPEAAYHD PYTQPSPGSV YSAQSAENPA AAFGVPGRVA SPYARSDTSS
TEAWRQRQAP GGGPGGLRRY ATRKVKLVQG SVLSVDYPVP SAIQNAIQAK YRNDLEGGSE
EFTHMRYTAA TCDPNEFTLH NGYNLRPAMY NRHTELLIAI TYYNEDKTLT SRTLHGVMQN
IRDIVNLKKS EFWNKGGPAW QKIVVCLVFD GIDPCDKDTL DVLATIGVYQ DGVMKRDVDG
KETVAHIFEY TTQLSVTPNQ QLIRPTDDGP STLPPVQMMF CLKQKNSKKI NSHRWLFNAF
GRILNPEVCI LLDAGTKPGP KSLLSLWEAF YNDKDLGGAC GEIHAMLGKG WKNLINPLVA
AQNFEYKISN ILDKPLESSF GYVSVLPGAF SAYRFRAIMG RPLEQYFHGD HTLSKQLGKK
GIEGMNIFKK NMFLAEDRIL CFELVAKAGS KWHLTYVKAS KAETDVPEGA PEFISQRRRW
LNGSFAAGIY SLMHFGRMYK SGHNIVRMFF LHIQMLYNIF STVLTWFSLA SYWLTTTVIM
DLVGTPSDNN GNKAFPFGKT ATPIINTIVK YVYLGFLLLQ FILALGNRPK GSKFSYLASF
VVFGIIQVYV VIDALYLVVR AFSGSAPMDF TTDQGVGEFL KSFFSSSGAG IIIIALAATF
GLYFVASFMY LDPWHMFTSF PAYMCVQSSY INILNVYAFS NWHDVSWGTK GSDKADALPS
AKTTKDEGKE VVIEEIDKPQ ADIDSQFEAT VKRALTPYVP PVEKEEKTLE DSYKSFRTRL
VTFWIFSNAF LAVCITSDGV DKFGFTNSAT DRTQRFFQAL LWSNAVVALF RFIGACWFLG
KTGLMCCFAR R
