CHSD_ASPFU
ID CHSD_ASPFU Reviewed; 745 AA.
AC P78746; Q4WSJ0; Q6MYM5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Chitin synthase D;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase D;
DE AltName: Full=Class-VI chitin synthase D;
GN Name=chsD; ORFNames=AfA5C5.045, AFUA_1G12600;
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=8807804; DOI=10.1111/j.1574-6968.1996.tb08463.x;
RA Mellado E., Specht C.A., Robbins P.W., Holden D.W.;
RT "Cloning and characterization of chsD, a chitin synthase-like gene of
RT Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 143:69-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA Barrell B.G., Hall N.;
RT "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT region encompassing the nitrate assimilation gene cluster.";
RL Fungal Genet. Biol. 41:443-453(2004).
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. {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 VI subfamily.
CC {ECO:0000305}.
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DR EMBL; U62614; AAB60781.1; -; Genomic_DNA.
DR EMBL; BX649606; CAF31978.1; -; Genomic_DNA.
DR EMBL; AAHF01000004; EAL90592.1; -; Genomic_DNA.
DR RefSeq; XP_752630.1; XM_747537.1.
DR AlphaFoldDB; P78746; -.
DR STRING; 746128.CADAFUBP00001186; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 3510460; -.
DR KEGG; afm:AFUA_1G12600; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_012773_0_0_1; -.
DR InParanoid; P78746; -.
DR OrthoDB; 240304at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 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..745
FT /note="Chitin synthase D"
FT /id="PRO_0000193681"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 613..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10..29
FT /note="Missing (in Ref. 3; EAL90592)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..20
FT /note="Missing (in Ref. 2; CAF31978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 84522 MW; B43B5D2B2D4A9632 CRC64;
MIVLFTLLRW APISPVFSMR TMHANLAHRG IFLPVMIVTL PLPVHLRRRF PAQMVLMLQW
FAFGMFSVLL IIPWLLCVYR LVTHSPGRTK RIKQVLDDRT APKTVVVMPV YKEAPETLIR
AIDSVVDCDY PANCIHVFLS YDGCLIDESY LRLIEHLGIP ITLESYPQSI DVTYKDARIT
VSRFKHGGKR HCQKQTFRLI DMVYADYLER HDNLFVLFID SDCILDRVCL QNFMYDMELK
PGSKHDMLAM TGVITSTTDR GSLLTLLQDM EYVHGQLFER SVESSCGAVT CLPGALTMLR
FSAFRKMAKY YFADKAEQCE DFFDYGKCHL GEDRWLTHLF MVGARKRYQI QMCAGAFCKT
EAVQTFSSLL KQRRRWFLGF ITNEVCMLTD VRLWKRYPLL CLVRFMQNTI RTTALLFFII
ALSLITTSSS INDLPVGFIA ISLGLNYVLM FYLGAKLKRY KAWLFPLMFI LNPFFNWLYM
VYGILTAGQR TWGGPRADAA TADEHTSPEE AVELAKAQGD ELNVDLTTFR SRGDEKSVPI
HPSEKIDGRF SAPELPDGYD SNLNDSNAAL TELMTPLPSV PRIGIHTYPS SDSILTSDSL
SSIHLPLKVE ELTGDNDNMK PYPDRQPRDT SSLHQMQRTC SNGIVASDSC SSQDDASEMV
NKPEILSPSA HILPHPSQAT ESSSGEDIYP LHLPSPHQHE AHFAPLNAST RGSMEGNTPE
VQRPRRKLPG IPRPIRAQKD PESMV
