ID   Q54276_SERMA            Unreviewed;       499 AA.
AC   Q54276;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:CAA85292.1};
DE   Flags: Precursor;
GN   Name=chiB {ECO:0000313|EMBL:CAA85292.1};
OS   Serratia marcescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615 {ECO:0000313|EMBL:CAA85292.1};
RN   [1] {ECO:0000313|EMBL:CAA85292.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Loeffler M.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAA85292.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7894703;
RA   Brurberg M.B., Eijsink V.GH., Haandrikman A.J., Venema G., Nes I.F.;
RT   "Chitinase B from Serratia marcescens BJL200 is exported to the periplasm
RT   without processing.";
RL   Microbiology 141:123-131(1995).
RN   [3] {ECO:0007829|PDB:1E15}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=10823940; DOI=10.1073/PNAS.97.11.5842;
RA   van Aalten D.M., Synstad B., Brurberg M.B., Hough E., Riise B.W.,
RA   Eijsink V.G., Wierenga R.K.;
RT   "Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-
RT   A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5842-5847(2000).
RN   [4] {ECO:0007829|PDB:1E6P, ECO:0007829|PDB:1E6R}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP   N-ACETYL-D-GLUCOSAMINE, AND DISULFIDE BONDS.
RX   PubMed=11481469; DOI=10.1073/PNAS.151103798;
RA   van Aalten D.M., Komander D., Synstad B., Gaseidnes S., Peter M.G.,
RA   Eijsink V.G.;
RT   "Structural insights into the catalytic mechanism of a family 18 exo-
RT   chitinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8979-8984(2001).
RN   [5] {ECO:0007829|PDB:1GPF}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=11836123; DOI=10.1016/S0968-0896(01)00372-8;
RA   Tabudravu J.N., Eijsink V.G., Gooday G.W., Jaspars M., Komander D.,
RA   Legg M., Synstad B., van Aalten D.M.;
RT   "Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge
RT   Aplysinella rhax.";
RL   Bioorg. Med. Chem. 10:1123-1128(2002).
RN   [6] {ECO:0007829|PDB:1UR8, ECO:0007829|PDB:1UR9}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-498 IN COMPLEX WITH
RP   N-ACETYL-D-GLUCOSAMINE, AND DISULFIDE BONDS.
RX   PubMed=14597613; DOI=10.1074/JBC.M310057200;
RA   Vaaje-Kolstad G., Vasella A., Peter M.G., Netter C., Houston D.R.,
RA   Westereng B., Synstad B., Eijsink V.G., van Aalten D.M.;
RT   "Interactions of a family 18 chitinase with the designed inhibitor HM508
RT   and its degradation product, chitobiono-delta-lactone.";
RL   J. Biol. Chem. 279:3612-3619(2004).
RN   [7] {ECO:0007829|PDB:1W1P, ECO:0007829|PDB:1W1T}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=15509170; DOI=10.1021/JM049940A;
RA   Houston D.R., Synstad B., Eijsink V.G., Stark M.J., Eggleston I.M.,
RA   van Aalten D.M.;
RT   "Structure-based exploration of cyclic dipeptide chitinase inhibitors.";
RL   J. Med. Chem. 47:5713-5720(2004).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; Z36295; CAA85292.1; -; Genomic_DNA.
DR   PIR; S52422; S52422.
DR   RefSeq; WP_004936562.1; NZ_MSEC01000014.1.
DR   PDB; 1E15; X-ray; 1.90 A; A/B=1-499.
DR   PDB; 1E6P; X-ray; 1.70 A; A/B=1-499.
DR   PDB; 1E6R; X-ray; 2.50 A; A/B=1-499.
DR   PDB; 1E6Z; X-ray; 1.99 A; A/B=2-499.
DR   PDB; 1GPF; X-ray; 1.85 A; A/B=1-499.
DR   PDB; 1UR8; X-ray; 1.90 A; A/B=1-499.
DR   PDB; 1UR9; X-ray; 1.80 A; A/B=1-499.
DR   PDB; 1W1P; X-ray; 2.10 A; A/B=1-499.
DR   PDB; 1W1T; X-ray; 1.90 A; A/B=1-499.
DR   PDB; 1W1V; X-ray; 1.85 A; A/B=1-499.
DR   PDB; 1W1Y; X-ray; 1.85 A; A/B=1-499.
DR   PDBsum; 1E15; -.
DR   PDBsum; 1E6P; -.
DR   PDBsum; 1E6R; -.
DR   PDBsum; 1E6Z; -.
DR   PDBsum; 1GPF; -.
DR   PDBsum; 1UR8; -.
DR   PDBsum; 1UR9; -.
DR   PDBsum; 1W1P; -.
DR   PDBsum; 1W1T; -.
DR   PDBsum; 1W1V; -.
DR   PDBsum; 1W1Y; -.
DR   PDBsum; 6JK9; -.
DR   PDBsum; 6JKF; -.
DR   AlphaFoldDB; Q54276; -.
DR   SMR; Q54276; -.
DR   DrugBank; DB04520; (3s,8ar)-3-(4-Hydroxybenzyl)Hexahydropyrrolo[1,2-a]Pyrazine-1,4-Dione.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   BRENDA; 3.2.1.14; 5690.
DR   BRENDA; 3.2.1.200; 5690.
DR   EvolutionaryTrace; Q54276; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd12204; CBD_like; 1.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; 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:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1E15, ECO:0007829|PDB:1E6P};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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}.
FT   DOMAIN          6..425
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DISULFID        328..331
FT                   /evidence="ECO:0007829|PDB:1E15, ECO:0007829|PDB:1E6P"
SQ   SEQUENCE   499 AA;  55469 MW;  58C933A9064D526B CRC64;
     MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS FLDINSNLEC
     AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS NDLGVSHANY VNAVKTPASR
     AKFAQSCVRI MKDYGFDGVD IDWEYPQAAE VDGFIAALQE IRTLLNQQTI TDGRQALPYQ
     LTIAGAGGAF FLSRYYSKLA QIVAPLDYIN LMTYDLAGPW EKVTNHQAAL FGDAAGPTFY
     NALREANLGW SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS
     GGNGGQYSSH STPGEDPYPS TDYWLVGCEE CVRDKDPRIA SYRQLEQMLQ GNYGYQRLWN
     DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV MFWHLGQDNR NGDLLAALDR
     YFNAADYDDS QLDMGTGLRY TGVGPGNLPI MTAPAYVPGT TYAQGALVSY QGYVWQTKWG
     YITSAPGSDS AWLKVGRVA
//