ID   CHIT_SACEN              Reviewed;         326 AA.
AC   P14529; A4F8N3;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Chitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=chiA2; OrderedLocusNames=SACE_1076;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-326.
RX   PubMed=2670919; DOI=10.1093/oxfordjournals.jbchem.a122791;
RA   Kamei K., Yamamura Y., Hara S., Ikenama T.;
RT   "Amino acid sequence of chitinase from Streptomyces erythraeus.";
RL   J. Biochem. 105:979-985(1989).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; AM420293; CAM00408.1; -; Genomic_DNA.
DR   PIR; JX0076; JX0076.
DR   RefSeq; WP_009946603.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; P14529; -.
DR   SMR; P14529; -.
DR   STRING; 405948.SACE_1076; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblBacteria; CAM00408; CAM00408; SACE_1076.
DR   KEGG; sen:SACE_1076; -.
DR   eggNOG; COG3469; Bacteria.
DR   HOGENOM; CLU_019399_0_1_11; -.
DR   OMA; TWTRIRD; -.
DR   OrthoDB; 1081028at2; -.
DR   Proteomes; UP000006728; Chromosome.
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   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:2670919"
FT   CHAIN           36..326
FT                   /note="Chitinase"
FT                   /id="PRO_0000077044"
FT   DOMAIN          40..326
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        80..124
FT   DISULFID        300..307
FT   CONFLICT        161
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  34023 MW;  5A9060DF8D8F79A1 CRC64;
     MGKLRKNLLA WAGTGVAAAC AVTMTAVPAL STPEPEAAGV VSASPYLYNG WGNPPSPTEV
     MNASGIKNFT LAFILADGTC NPAWDGNRPL DGQDKATIDA IRGAGGDVIP SIGGYSGSKL
     GEVCQDSQSL AGAYQKVIDA YGLKAIDVDI EATEFENDAS QTRVLEALKI VKEANPGLRT
     VVTFPTLVNG PNDVGKRMID KAARIGSDVD VWTQMPFNFG GGDMAADTIT STEGLVAHLK
     SAFGYDDATA YAHAGISSMN GKSDTGETVD QAAFQKMADY AGEKGLGRLS FWSVNRDRPC
     DGAPDACGGI DQQPWDFTKI VAGLQS