CHSC_ASPFU
ID CHSC_ASPFU Reviewed; 893 AA.
AC Q92197; Q4WDV2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chitin synthase C;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase C;
DE AltName: Full=Class-III chitin synthase C;
GN Name=chsC; ORFNames=AFUA_5G00760;
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 [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. {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. Class III subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL86225.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X94245; CAA63929.1; -; Genomic_DNA.
DR EMBL; AAHF01000011; EAL86225.1; ALT_SEQ; Genomic_DNA.
DR PIR; JC6015; JC6015.
DR RefSeq; XP_748263.1; XM_743170.1.
DR AlphaFoldDB; Q92197; -.
DR STRING; 746128.CADAFUBP00004815; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; Q92197; -.
DR GeneID; 3505740; -.
DR KEGG; afm:AFUA_5G00760; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_0_1_1; -.
DR InParanoid; Q92197; -.
DR OrthoDB; 256142at2759; -.
DR BRENDA; 2.4.1.16; 517.
DR PHI-base; PHI:3047; -.
DR PHI-base; PHI:564; -.
DR Proteomes; UP000002530; Chromosome 5.
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; IEA:UniProt.
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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..893
FT /note="Chitin synthase C"
FT /id="PRO_0000193680"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29
FT /note="Missing (in Ref. 2; EAL86225)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="L -> R (in Ref. 1; CAA63929)"
FT /evidence="ECO:0000305"
FT CONFLICT 633..636
FT /note="Missing (in Ref. 1; CAA63929)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="G -> A (in Ref. 1; CAA63929)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="A -> R (in Ref. 1; CAA63929)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="N -> S (in Ref. 1; CAA63929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 101041 MW; 193A30241858960A CRC64;
MGTPRPYSAH SPQESRSSFY SQPSQSPTQP TYGRDDAEDQ QQSLLRRSLA SPNGWSYDDP
NVSTDSLRRY TLHDPGITAF APPYPESEAA DVRSARMSGY SGIEMDAWQR RQGVKPSALR
RYGTRKINLV QGSVLSVDYP VPSAIQNAIQ AEYRDAEEAF HEEFTHMRYT AATCDPDEFT
LRNGYNLRPA MYNRHTELLI AITYYNEDKV LTARTLHGVM QNVRDIVNLK KSEFWNKGGP
AWQKIVVCLV FDGIEPCDKN TLDVLATIGV YQDGVMKKDV DGRETVAHIF EYTTQLSVTP
TQQLVRPQPN DPSNLPPVQM LFCLKQKNSK KINSHRWLFN AFSRILNPEI CILLDAGTKP
GSKSLLALWE AFYNDKTLGG ACGEIHAMLG RGWRNVLNPL VAAQNFEYKI SNILDKPLES
AFGYVSVLPG AFSAYRYRAI MGRPLEQYFH GDHTLSKRLG KKGIEGMNIF KKNMFLAEDR
ILCFELVAKA GYKWHLTYVK ASKGETDVPE AAPEYISQRR RWLNGSFAAS LYSIMHFGRI
YKSGHSFVRM FFLHIQMIYN CCQLIMTWFS LASYWLTSSV IMDLVGTPSS HNKYKAWPFG
NDASPIVNFF VKYGYLLVLM LQFVLALGNR PKGTKLAYTM SFLWFSLVQF YVLILSFYLV
ANAFMGGMID FDFDQGVGNF LSSFFSSTGG GIVLIALVST YGIYIVASIL YMDPWHILTS
SWAYFLGMTT SINILMVYAF CNWHDVSWGT KGSDKADALP SAQTKKADGS KSNFIEEIDK
PQADIDSQFE ATVKRALAPY QEPKEDSTIS LDDSYRNFRT SLVLLWILSN LLVSLLITND
GIRKMCLTNT STTRTQYYFQ VILWATAGLS IFRFIGSIYF LGKSGILCCV TRR
