ID Q5AQP0_EMENI Unreviewed; 1132 AA.
AC Q5AQP0; C8VRJ3;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=ANIA_09390 {ECO:0000313|EMBL:CBF87524.1};
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 {ECO:0000313|EMBL:CBF87524.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., 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 [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; BN001308; CBF87524.1; -; Genomic_DNA.
DR RefSeq; XP_682659.1; XM_677567.1.
DR AlphaFoldDB; Q5AQP0; -.
DR SMR; Q5AQP0; -.
DR STRING; 227321.Q5AQP0; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblFungi; CBF87524; CBF87524; ANIA_09390.
DR GeneID; 2867869; -.
DR KEGG; ani:AN9390.2; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_001837_0_0_1; -.
DR InParanoid; Q5AQP0; -.
DR OMA; CWTGHKS; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd06922; ChtBD1_GH18_1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1132
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010306783"
FT DOMAIN 76..128
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 130..486
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 93..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 98..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1132 AA; 124695 MW; C7E0D1EE9870AC2F CRC64;
MSKDLQRFNM LLLYCSRFHL CVLAALICLA IVSAQQDYSC SPVRPCKLGC CGKNNVCGMG
PSYCASENCT STCDAKSECD PGWGSQWSQR QSCPLNVCCS KYGFCGTTEE FCGDEKVTKP
SCPGGTSASK KVIGYYEGWS TSKKCNGLNP EDLLMGAYTH LNYAFAFIDP ESYKIANMQD
SDEEYMPRLT ALKNYNPSLE VWIAIGGWSM NDPDQPTRRT FSELAASKSH QDVFFESLLS
FMDKYGFDGV DIDWEYPVAE ERSGAPEDFE NYVSFLKNLR AVLGNRGLTI TLPASFWYLQ
HFDIKNMEPI LDWFNIMSYD LHGTWDGTNP YLGPYINSHT NLTEIDLAME LLWRNDIDPK
KVVMGMGFYG RSFTLSDPAC NTPGCGFSAG GNPGKCSASA GSLMFSEIQE IIDAGGAKVT
NDEKAGVQMV TWDTNQWVSY DDDETLKAKM EYANELCLGG VMVWAASTDD HKGTAIRALA
KAAGRTDLTV PVLAAKANND PSQCVWGECG ADCPSGLIPV EESSSNKNPL GIELGCNQGT
RYFCCPSKSP PTCKWKGSPK FCGLLSKNRC TDDEIEVSAS TEGCWTGHKS LCCTKTESTD
VLDACKWFGA APICAASAFF PSLLGPLGGA FSFHSYGCDD DDNRPNELTK AKQGQGGQQS
CTYNGGFKSF CCENPTPWKD CKWRAGNTAW VQWENLLFGP IGALFFDFST DCKTGCEPGE
TTVATDGWGC RSGTYSYFCC ADPNQPASPD LPDINLCYGP NHLDSLTSDL EGESNLPNVY
EEETVFDYGC GTDDLTALLK GKRGTEDVAF ASNLSQLAVL ETSPFLLEEH DLVPRGARER
IAMALCGPNG QRSSIWVQQY PGASSILLAT GRAWTVAKQG LCAAAGITSL STLASNTDWV
TEHVLEKQEF RNALEYMAAG QTPSGTMLRS GAVPFAQVFG NNGIFQQSWP TVTYPTLTFT
HNLVGNINDF FTGLLGRTSD PGLSNRFIEN LQVCDRDFNV YKEYMVKGAD FISRTMWSNY
NPQERVVAAF SSTYKNIATM FKDLTRYAAT QGITYDFEDA WKQIMPDYLN WQVERVRDTF
ETYVDEEILY WASSLAQNTY APLVIKEMSD LLQDLKTNMN TLLALPVTQM TS
//
