ID B6GXQ2_PENRW Unreviewed; 1851 AA.
AC B6GXQ2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=Pc12g11730 {ECO:0000313|EMBL:CAP80800.1}, PCH_Pc12g11730
GN {ECO:0000313|EMBL:CAP80800.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP80800.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP80800.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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:0000256|ARBA:ARBA00024009}.
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:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AM920427; CAP80800.1; -; Genomic_DNA.
DR RefSeq; XP_002557990.1; XM_002557944.1.
DR STRING; 500485.B6GXQ2; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 8307566; -.
DR KEGG; pcs:Pc12g11730; -.
DR VEuPathDB; FungiDB:PCH_Pc12g11730; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR BioCyc; PCHR:PC12G11730-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036037; MYSc_Myo17.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR SMART; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 890..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..949
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1591..1614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1626..1645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1793..1848
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1851 AA; 205599 MW; DFFE68EFA943AA0E CRC64;
MVNTFSGSGP AHAQPSLPSL PAHLQSDTHL TAHLASRFHV GLPTAHLSSQ ALIALNTYTS
ATKGPDGGKE GSAAGEAEDL ARRAFTRLGA RAENQAVVFL GESGSGKTTI RSHLLSSFLS
FSSTPLSSKL SYAAFVFDTL TTTKSVTTPT ASKAGLFLEL QYDGSSSVNP TLIGGKIIDY
RLERSRISSV PTGERSFHVL YYLLAGTSAA EKSHLGFENS IHVQTGSRLS GGTVSHKRWR
YLGHPTQLKV GINDTEGFQH FKTALRKLEF SRGEIAEICQ ILASILHIGQ LEFATGQSTT
TGAEESGGYS HEGGETVTVV KNKDVLDNVA AFLGLSVDAL ENSLGYRTKT IHRERVTVML
DPKGARENAD AFARTIYSLL VTYVIETVNQ RLCAAEDSVA NTISIVDFPG FAQAPSTGST
LDQLLSNAAT ESLYNYCLQS FFDHKADILD REEITVAATS YFDNTDTVRG LLKHGNGLLS
ILDDQTRRGR SDAQFLESVR KRFENKNPAI SVGGTSGSGG YMSQTRSAFT VKHFAGEVDY
STTGLLEENG EVISGDLMNL VRSTRSDFVR ELFHQEALQT ISHPQEKTAI MQAQVSSKPL
RMPSMARRKT GPPSRFAAPS AHPESEEGDE HESQVAGKRA NGRKSGMPSG PAQGAAGQFL
SGLEIVNKCL SSSNLNPYFV ICLKPNDRRI ANQFDSKCVR MQVQTFGIAE ISSRLRNADY
SVFLPFGEFL GLAEIGNVVV GSDREKSEVV LDEKRWPGNE ARVGSTGVFL SERCWADIAK
VGERVVPSYG NAGADEGDGF QAAGGNPDSK LRLLHPTDQS PGAFIYGEDP KQGYFGSREL
DGRSDAGGSA FNSGDMFKNL DTKEQMLEKN NEKKMEEVDE APTSAGRRRW MFLVYLLTFF
IPDFVIRFVG RMKRKDVRIA WREKLAINMI IWFACGVAVF MIVGFPGVVC PTQDVYNTAE
LSGKNGQGSA ESYVSIRGVV FNLGNFMPSH FPDIVPQKSL KAYAGTDATN LFPIQVSALC
QGVNGKVDAS VPLDYRSNLN DSAVTASSST FDVNAKYHDF RSWTNDSRAD WFYEQMLMMR
SNYKKGYVGY TSKAIKKLAI DDSKKVVSIH GKVYDMTYYI AGPRVPRWPA GKNGTGNVDT
DYMSPLIVDI FQGKPGEDVS KYWDELNFDT ALRSRMQLCL DNLFFIGKVD TRDSVRCQFA
RYFILAISIM LVSIIGFKFL AALQFGKKNL PENLDKFIIC QVPVYTEDEE SLRRAMDSMA
RMRYDDKRKL LLVICDGMII GQGNDRPTPR IVLDILGVPE SVDPEPLSFE SLGEGMKQHN
MAKIYSGLYE VQGHIVPFLV VVKVGKPSEV SRPGNRGKRD SQMVLMRFLN RVHYNLPMSP
MELEMHHHIR NIIGVNPQFY EYILQVDADT MVAPDAATRF VSAFLSDTRL IGCCGETSLS
NAKTSIVTMI QVYEYYISHN LTKAFESLFG SVTCLPGCFT MYRIRTAENG TPLFVSKAVV
DSYSEIRVDT LHMKNLLHLG EDRYLTTLLL KHHPKFKTKY IFRCHAWTVA PESFTVFLSQ
RRRWINSTVH NLMELIPLQQ LCGFCCFSMR FIVLIDLLMT VIQPVTVAYI AYLIYWCVSE
PDVLPITSFI LLGVIYGLQA LIFLVRRKWE MIVWMLIYLL AIPIFSLALP LYSFWHMDDF
SWGNTRVITG EKGRKVVISD EGKFDPDSIP KKIWEDYQAE LWESQTSRDD RSEFSAHSYG
TRLPPFPQSE YGFHTGSRPV SQLDLPLGGG GTRYSVTPSE MMSNFGMEDL SHLPPDDEIL
EEIRKILATA DLMKVSKKTV KQELERRFDV NLDAKRPYIN SATEAVLSGV L
//
