CHSD_EMENI
ID CHSD_EMENI Reviewed; 1194 AA.
AC P78611; C8VMZ3; Q00744; Q5BD25;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 4.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Chitin synthase D;
DE EC=2.4.1.16 {ECO:0000269|PubMed:8810520};
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase D;
DE AltName: Full=Class-V chitin synthase D;
GN Name=chsD; Synonyms=chsE; ORFNames=AN1555;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC 89;
RX PubMed=8709948; DOI=10.1007/bf02172373;
RA Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RT "The Aspergillus nidulans genes chsA and chsD encode chitin synthases which
RT have redundant functions in conidia formation.";
RL Mol. Gen. Genet. 251:442-450(1996).
RN [2]
RP ERRATUM OF PUBMED:8709948.
RX PubMed=9037115; DOI=10.1007/s004380050353;
RA Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RL Mol. Gen. Genet. 253:520-528(1997).
RN [3]
RP SEQUENCE REVISION.
RA Motoyama T., Fujiwara M., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=8810520; DOI=10.1006/fgbi.1996.0030;
RA Specht C.A., Liu Y., Robbins P.W., Bulawa C.E., Iartchouk N., Winter K.R.,
RA Riggle P.J., Rhodes J.C., Dodge C.L., Culp D.W., Borgia P.T.;
RT "The chsD and chsE genes of Aspergillus nidulans and their roles in chitin
RT synthesis.";
RL Fungal Genet. Biol. 20:153-167(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 Evidence={ECO:0000269|PubMed:8810520};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class V subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA11866.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA64262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D83246; BAA11866.2; ALT_SEQ; Genomic_DNA.
DR EMBL; U52362; AAA97482.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000025; EAA64262.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF85100.1; -; Genomic_DNA.
DR PIR; JC6079; JC6079.
DR RefSeq; XP_659159.1; XM_654067.1.
DR AlphaFoldDB; P78611; -.
DR STRING; 162425.CADANIAP00008183; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; CBF85100; CBF85100; ANIA_01555.
DR EnsemblFungi; EAA64262; EAA64262; AN1555.2.
DR GeneID; 2875763; -.
DR KEGG; ani:AN1555.2; -.
DR VEuPathDB; FungiDB:AN1555; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_1_0_1; -.
DR InParanoid; P78611; -.
DR OMA; DIMGLCG; -.
DR OrthoDB; 134286at2759; -.
DR BRENDA; 2.4.1.16; 517.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0045009; C:chitosome; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
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:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0004100; F:chitin synthase activity; IMP:AspGD.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IGI:AspGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006031; P:chitin biosynthetic process; IMP:AspGD.
DR GO; GO:0048315; P:conidium formation; IGI:AspGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1194
FT /note="Chitin synthase D"
FT /id="PRO_0000193693"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1097..1117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 606
FT /note="L -> S (in Ref. 1; BAA11866 and 4; AAA97482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 134864 MW; 5CFA527B791118B6 CRC64;
MSLPQRPGKT SPRREETSAF REPSRRRRRE SDSLSNNDPT SPRHHRHHRS HSSRHQHDID
EERAEEGGIR RKRSLVKPER GRMDPSHPNY LYRQKTQNMP TYNPMTGNEP LIHEEGEAET
NSTPSMDSKR KDALYGAHGN VNKPMERVPT RHRSKKRKGS RKISKREAAA EKRRRKAMEQ
VRPPSLWTTY CSVITFWAPD FVLKCFGMPQ KAQRSAWREK IGLISIILMI AAFVGFLTFG
FTATVCGTPP TRLKINEIGS GYMIFHGQAY DLTKSTHPAA AGIPDMTNVL YDLPHKYGGQ
DGSFFFQEVN GACKGLITRT ENSDIPTNSN GDLAWYFPCH AFNQDGSSEP NTTVSYYNGW
ACHTSGSARK SFYSLKNSGD VYFTWEDTKN TSRKLAVYSG NVLDLNLLNW FDDTQVNYPT
KFKDLRDNDD IRGVDLTYYF QTGEDKQIGK CLSQIIKVGS IDTDTVGCIA SQVVLYVSLI
FILSIVIVKF AFALLFQWFL APRFAAQKTS MGAVDSKARN QQIEDWSNDI YRPGPRLADP
VPGDRMSKRA SFLPTTSRFS SPYTVSNGGK QKPQWVTMAS QNSTTRLVPP ASGTTPSIYR
QSHNGLGNVS VDNSRLNPSA SRTSLVQDSR YSTVIPDSEG IGSAGYVHEL VVPQPPPDWQ
PYGFPLAHAM CLVTCYSEGE EGIRTTLDSI ALTDYPNSHK SIVVICDGII KGKGEEFSTP
DIVLRMMRDP IIPPEEVEAF SYVAVATGSK RHNMAKVYAG FYDYGEHSII PVEKQQRVPM
MIIVKCGTPA EATAAKPGNR GKRDSQIILM SFLQKVMFDE RMTELEYEMF NGLLHVTGIP
PDFYEVVLMV DADTKVFPDS LTHMISAMVK DPEVMGLCGE TKIANKTDSW VTMIQVFEYF
VSHHQSKAFE SVFGGVTCLP GCFSMYRIKA PKGGQNYWVP ILANPDIVEH YSENVVDTLH
KKNLLLLGED RYLSTLMLRT FPKRKQIFVP QAVCKTVVPD KFMVLLSQRR RWINSTVHNL
MELVLVRDLC GTFCFSMQFV IFVELVGTVV LPAAISFTIY VVVSSIIKQP VQIIPLVLLA
LILGLPGVLV VVTAHRLVYV LWMLVYLISL PIWNFVLPTY AYWKFDDFSW GDTRKTAGEK
DKGHEDGEGE FDSSKITMKR WRDFEKDRRL RMQAGWQLPV GGHPPMPYEP YPEY
