CHIA_SERMA
ID CHIA_SERMA Reviewed; 563 AA.
AC P07254; Q54275;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Chitinase A;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=chiA;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Koo J.C., Lim C.O., Choi Y.J., Kim C.Y., Bahk J.D., Lee S.Y., Cho M.J.;
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 990 / QMB1466;
RX PubMed=16453672; DOI=10.1002/j.1460-2075.1986.tb04235.x;
RA Jones J.D.G., Grady K.L., Suslow T.V., Bedbrook J.R.;
RT "Isolation and characterization of genes encoding two chitinase enzymes
RT from Serratia marcescens.";
RL EMBO J. 5:467-473(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-31.
RC STRAIN=BJL200;
RX PubMed=7851747; DOI=10.1111/j.1574-6968.1994.tb07315.x;
RA Brurberg M.B., Eijsink V.G.H., Nes I.F.;
RT "Characterization of a chitinase gene (chiA) from Serratia marcescens
RT BJL200 and one-step purification of the gene product.";
RL FEMS Microbiol. Lett. 124:399-404(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=7704527; DOI=10.1016/s0969-2126(94)00119-7;
RA Perrakis A., Tews I., Dauter Z., Oppenheim A.B., Chet I., Wilson K.S.,
RA Vorgias C.E.;
RT "Crystal structure of a bacterial chitinase at 2.3-A resolution.";
RL Structure 2:1169-1180(1994).
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; L01455; AAA26551.1; -; Genomic_DNA.
DR EMBL; X03657; CAA27292.1; -; Genomic_DNA.
DR EMBL; Z36294; CAA85291.1; -; Genomic_DNA.
DR PIR; A25090; A25090.
DR PIR; S60651; S60651.
DR RefSeq; WP_021504113.1; NZ_VKVH01000016.1.
DR PDB; 1CTN; X-ray; 2.30 A; A=24-563.
DR PDB; 1EHN; X-ray; 1.90 A; A=24-563.
DR PDB; 1EIB; X-ray; 1.80 A; A=24-563.
DR PDB; 1FFQ; X-ray; 1.90 A; A=24-563.
DR PDB; 1FFR; X-ray; 1.80 A; A=24-563.
DR PDB; 1K9T; X-ray; 1.80 A; A=24-563.
DR PDB; 1NH6; X-ray; 2.05 A; A=24-563.
DR PDB; 1RD6; X-ray; 2.60 A; A=1-563.
DR PDB; 1X6L; X-ray; 1.90 A; A=1-563.
DR PDB; 1X6N; X-ray; 2.00 A; A=1-563.
DR PDB; 2WK2; X-ray; 2.05 A; A=24-563.
DR PDB; 2WLY; X-ray; 2.40 A; A=24-563.
DR PDB; 2WLZ; X-ray; 1.82 A; A=24-563.
DR PDB; 2WM0; X-ray; 1.90 A; A=24-563.
DR PDB; 5Z7M; X-ray; 2.00 A; A=24-563.
DR PDB; 5Z7N; X-ray; 1.70 A; A=24-563.
DR PDB; 5Z7O; X-ray; 2.00 A; A=24-563.
DR PDB; 5Z7P; X-ray; 2.00 A; A=24-563.
DR PDBsum; 1CTN; -.
DR PDBsum; 1EHN; -.
DR PDBsum; 1EIB; -.
DR PDBsum; 1FFQ; -.
DR PDBsum; 1FFR; -.
DR PDBsum; 1K9T; -.
DR PDBsum; 1NH6; -.
DR PDBsum; 1RD6; -.
DR PDBsum; 1X6L; -.
DR PDBsum; 1X6N; -.
DR PDBsum; 2WK2; -.
DR PDBsum; 2WLY; -.
DR PDBsum; 2WLZ; -.
DR PDBsum; 2WM0; -.
DR PDBsum; 5Z7M; -.
DR PDBsum; 5Z7N; -.
DR PDBsum; 5Z7O; -.
DR PDBsum; 5Z7P; -.
DR AlphaFoldDB; P07254; -.
DR SMR; P07254; -.
DR STRING; 273526.SMDB11_4243; -.
DR BindingDB; P07254; -.
DR ChEMBL; CHEMBL5423; -.
DR DrugBank; DB03109; 2-acetylamino-2-deoxy-b-D-allopyranose.
DR DrugBank; DB04628; Allosamidin.
DR DrugBank; DB04404; Allosamizoline.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; P07254; -.
DR GeneID; 66716875; -.
DR BioCyc; MetaCyc:MON-17691; -.
DR BRENDA; 3.2.1.14; 5690.
DR BRENDA; 3.2.1.201; 5690.
DR SABIO-RK; P07254; -.
DR EvolutionaryTrace; P07254; -.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
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; SM00636; Glyco_18; 1.
DR SMART; SM00089; PKD; 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 3D-structure; Carbohydrate metabolism; Chitin degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7851747"
FT CHAIN 24..563
FT /note="Chitinase A"
FT /id="PRO_0000011908"
FT DOMAIN 158..559
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CONFLICT 52
FT /note="N -> S (in Ref. 3; CAA85291)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> T (in Ref. 3; CAA85291)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..77
FT /note="TA -> GP (in Ref. 2; CAA27292)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="I -> V (in Ref. 3; CAA85291)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="T -> S (in Ref. 3; CAA85291)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> P (in Ref. 2; CAA27292)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="V -> I (in Ref. 2; CAA27292)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="P -> A (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..429
FT /note="PAWKPDTAYTTVNGVNALLA -> RPGSRHRLHHGERRQCAAG (in Ref.
FT 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="V -> I (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..467
FT /note="ATGP -> HRA (in Ref. 2; CAA27292)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="K -> E (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="G -> S (in Ref. 2; CAA27292)"
FT /evidence="ECO:0000305"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1EIB"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1CTN"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:5Z7N"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:5Z7N"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:5Z7N"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 331..353
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:1EHN"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 420..430
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 479..485
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:5Z7N"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:5Z7N"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 518..531
FT /evidence="ECO:0007829|PDB:5Z7N"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:5Z7N"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:5Z7N"
SQ SEQUENCE 563 AA; 60979 MW; 0696FEF6AF83AA35 CRC64;
MRKFNKPLLA LLIGSTLCSA AQAAAPGKPT IAWGNTKFAI VEVDQAATAY NNLVKVKNAA
DVSVSWNLWN GDAGTTAKIL LNGKEAWSGP STGSSGTANF KVNKGGRYQM QVALCNADGC
TASDATEIVV ADTDGSHLAP LKEPLLEKNK PYKQNSGKVV GSYFVEWGVY GRNFTVDKIP
AQNLTHLLYG FIPICGGNGI NDSLKEIEGS FQALQRSCQG REDFKVSIHD PFAALQKAQK
GVTAWDDPYK GNFGQLMALK QAHPDLKILP SIGGWTLSDP FFFMGDKVKR DRFVGSVKEF
LQTWKFFDGV DIDWEFPGGK GANPNLGSPQ DGETYVLLMK ELRAMLDQLS AETGRKYELT
SAISAGKDKI DKVAYNVAQN SMDHIFLMSY DFYGPFDLKN LGHQTALNAP AWKPDTAYTT
VNGVNALLAQ GVKPGKVVVG TAMYGRGWTG VNGYQNNIPF TGTATGPVKG TWKNGIVDYR
QIAGQFMSGE WQYTYDATAE APYVFKPSTG DLITFDDARS VQAKGKYVLD KQLGGLFSWE
IDADNGDILN SMNASLGNSA GVQ
