ID   CHIA_PSEO7              Reviewed;         820 AA.
AC   P32823;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Chitinase A;
DE            Short=CHI-A;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chiA;
OS   Pseudoalteromonas piscicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O-7;
RX   PubMed=8416892; DOI=10.1128/jb.175.1.176-181.1993;
RA   Tsujibo H., Orikoshi H., Tanno H., Fujimoto K., Miyamoto K., Imada C.,
RA   Okami Y., Inamori Y.;
RT   "Cloning, sequence, and expression of a chitinase gene from a marine
RT   bacterium, Altermonas sp. strain O-7.";
RL   J. Bacteriol. 175:176-181(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-48, AND CHARACTERIZATION.
RC   STRAIN=O-7;
RX   PubMed=1464065; DOI=10.1139/m92-145;
RA   Tsujibo H., Yoshida Y., Miyamoto K., Imada C., Okami Y., Inamori Y.;
RT   "Purification, properties, and partial amino acid sequence of chitinase
RT   from a marine Alteromonas sp. strain O-7.";
RL   Can. J. Microbiol. 38:891-897(1992).
RN   [3]
RP   MUTAGENESIS.
RC   STRAIN=O-7;
RX   PubMed=7764022; DOI=10.1271/bbb.57.1396;
RA   Tsujibo H., Orikoshi H., Imada C., Okami Y., Miyamoto K., Inamori Y.;
RT   "Site-directed mutagenesis of chitinase from Alteromonas sp. strain O-7.";
RL   Biosci. Biotechnol. Biochem. 57:1396-1397(1993).
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   -!- ACTIVITY REGULATION: Stimulated by magnesium ions; inhibited by N-
CC       bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0.;
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AB063629; BAB79620.1; -; Genomic_DNA.
DR   PIR; A40633; A40633.
DR   PIR; PC4106; PC4106.
DR   AlphaFoldDB; P32823; -.
DR   SMR; P32823; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.10.50.10; -; 1.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR013540; ChitinaseA_N.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   Pfam; PF08329; ChitinaseA_N; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SMART; SM00089; PKD; 2.
DR   SUPFAM; SSF51055; SSF51055; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1464065"
FT   CHAIN           22..820
FT                   /note="Chitinase A"
FT                   /id="PRO_0000011904"
FT   DOMAIN          158..588
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        313
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   820 AA;  87346 MW;  FFD70D91192BA320 CRC64;
     MKLNKITSYI GFALLSGGAL AAPSTPTLDW QPQQYSFVEV NVDGLGSYKQ LVKAKDVVDI
     SIKWNAWSGS GGDNYKVYFD DLLVNQGSLP AGTKSGVVQF PYTKSGRHQL YLELCEGTVC
     ARSAGKEIVI ADTDGAHLAP LPMNVDPNNR NNGTIPGRVT GAYFVEWGIY GRNYDVTKIP
     AHNLSHILYG FIPICGPNES LKSIEIGNSW RALQTACADS QDYEVVIHDP WAAVQKSMPG
     VDAKDPIRGV YSQLMALKQR YPDLKILPSV GGWTLSDPFH GFTNKANRDT FVASVKQFLK
     TWKFYDGVDI DWEFPGGDGP NPDLGDPIND GPAYVALMQE LRAMLDELEA ETGRQYELTS
     AIGAGYDKIE DVDYQAAQQY MDYIFAMTYD FYGAWNNETG HQTGIYCGSH LSTDECNGTG
     VDDNGVPRKG PAYTGDHAIQ LLLQQGVQPS KLVMGVAMYG RGWEGVLDAN AAIPGNPMTA
     PGNGPLTGST SEGVWEPGIM DYKAIAANAV GQGGSGVNGY EVGYDEQAQA AYVWNRSNGK
     LITYDSPRSV IAKGQYANTH QLAGLFGWEI DADNGDILNA MYDGLTAGEI PNRAPTIGVS
     GPINVTSGQV VNVDAQASDL DNDPLTYSWV AAPGLALSAN NTAAVAVTAP SVAQQTSYDL
     TVTVNDGALS TTKTIVVVVN PEGANAAPVV TPVSDISVNE GASATVNVSA TDPEGAALSY
     SWSVPAELSV ANGSSATITA ANVTADTTVP VTVTVSDGVN AVDTTFNVTI KDGAEYPTWD
     RSTVYVGGDR VIHNSNVFEA KWWTQGEEPG TADVWKAVTN