ID   CHSA_EMENI              Reviewed;        1013 AA.
AC   P30584; C8VB73; Q5AXE8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Chitin synthase A;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase A;
DE   AltName: Full=Class-II chitin synthase A;
GN   Name=chsA; Synonyms=chs2; ORFNames=AN7032;
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=7765508; DOI=10.1271/bbb.58.1828;
RA   Yanai K., Kojima N., Takaya N., Horiuchi H., Ohta A., Takagi M.;
RT   "Isolation and characterization of two chitin synthase genes from
RT   Aspergillus nidulans.";
RL   Biosci. Biotechnol. Biochem. 58:1828-1835(1994).
RN   [2]
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   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 303-491.
RX   PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA   Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA   Robbins P.W.;
RT   "Classification of fungal chitin synthases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
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 II subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA61678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; D21268; BAA04806.1; -; Genomic_DNA.
DR   EMBL; AACD01000117; EAA61678.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M82939; AAA33303.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79220.1; -; Genomic_DNA.
DR   PIR; JC2314; JC2314.
DR   RefSeq; XP_664636.1; XM_659544.1.
DR   AlphaFoldDB; P30584; -.
DR   STRING; 162425.CADANIAP00000441; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; CBF79220; CBF79220; ANIA_07032.
DR   EnsemblFungi; EAA61678; EAA61678; AN7032.2.
DR   GeneID; 2870113; -.
DR   KEGG; ani:AN7032.2; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   HOGENOM; CLU_045174_1_0_1; -.
DR   InParanoid; P30584; -.
DR   OMA; FIISMGN; -.
DR   OrthoDB; 256142at2759; -.
DR   BRENDA; 2.4.1.16; 517.
DR   Proteomes; UP000000560; Chromosome IV.
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: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; IGI:CACAO.
DR   GO; GO:0000918; P:division septum site selection; IGI:CACAO.
DR   GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
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..1013
FT                   /note="Chitin synthase A"
FT                   /id="PRO_0000193691"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        646..666
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        721..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        759..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        892..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        919..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          26..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  113679 MW;  DD5D2E9523B0778A CRC64;
     MDCQNGRRAN RTVRFARTAE SRYPERYSYE YDPEETLSRA APSMRNAPTI PPPTASGADE
     MRYTASRPAS PARPWSPTRA ADWVRPPSAA ASYYERADIN GSPRPGTPSS RYGGSPRRPL
     PPAPLFSKPG TTTQDTKIDI GDGEEDPFGG GGRTISSRHG PQGSVQSFTS ESTFIADETD
     LEKVDLDEYE EESNETKSMV DPNLHYGPAP EKQSRRGVRN AQMAKKEVQL VNGELILECK
     IPTILHSFLP RRDDREFTHM RYTAVTCDPD DFTQRGYKLR QQIGRTMRET ELFICITMYN
     EDETHFTRTM HGVMQNISHF CSRSKSRTWG KDGWKKIVVC IISDGRKKVH PRTLNALAAL
     GVYQEGIAKN VVNQKQVNAH VYEYTTQVSL DSDLKFKGAE KGIVPCQVIF CLKEHNQKKL
     NSHRWFFNAF GRALQPNICI LLDVGTRPEP TALYHLWKAF DQDSNVAGAA GEIKASKGKN
     MLGLLNPLVA SQNFEYKMSN ILDKPLESVF GYITVLPGAL SAYRFFALQN DAEGNGPLNQ
     YFKGETLHGK DADVFTANMY LAEDRILCWE LVAKREERWV LRFVKSAVGE TDVPDSIPEF
     ISQRRRWLNG AFFAAVYSIV NVKQLWKTDH SLARKILLQI ESVYQLLQLI FTYFGLANFY
     LAFFFIAGSL TDEKIDPFGH NMGKYIFIVL RYACVLVMCL QFIFSMGNRP QGAKKLYLSS
     MIVYSIVMAY TAFCTLYLIV LELMAKTGHD VPITMSDTLF VNIVVSLLST VGLYFFTSFM
     YLDPWHMFTS SAQYFALLPS YICTLQCYAF CNTHDVTWGT KGDNTINTDL GTARIINGSI
     VEVEMPSEQL DIDSGYDAAL RNLRDRLEVP DPGVSESQQQ EDYYRAVRTY MVSVWMVANV
     VLAMAVSEVY GVGSSGTNVY LAIILWSVAV LAIIRAIGST AYAVLYLIQK LVEGKAKFQA
     GNIASANASA AGSSLGTKSN VSYGSKGLNM TDRINETKWA ISRGMQKAMF WKK