CHIA1_NIACI
ID CHIA1_NIACI Reviewed; 699 AA.
AC P20533;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chitinase A1;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=chiA1;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WL-12;
RX PubMed=2203782; DOI=10.1016/s0021-9258(18)55449-1;
RA Watanabe T., Suzuki K., Oyanagi W., Ohnishi K., Tanaka H.;
RT "Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its
RT evolutionary relationship to Serratia chitinase and to the type III
RT homology units of fibronectin.";
RL J. Biol. Chem. 265:15659-15665(1990).
RN [2]
RP MUTAGENESIS.
RC STRAIN=WL-12;
RX PubMed=8103047; DOI=10.1016/s0021-9258(17)46665-8;
RA Watanabe T., Kohori K., Miyashita K., Fujii T., Sakai H., Uchida M.,
RA Tanaka H.;
RT "Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1
RT of Bacillus circulans WL-12 as essential residues for chitinase activity.";
RL J. Biol. Chem. 268:18567-18572(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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; M57601; AAA81528.1; -; Genomic_DNA.
DR PIR; A38368; A38368.
DR PDB; 1ED7; NMR; -; A=655-699.
DR PDB; 1ITX; X-ray; 1.10 A; A=33-451.
DR PDB; 1K85; NMR; -; A=559-644.
DR PDBsum; 1ED7; -.
DR PDBsum; 1ITX; -.
DR PDBsum; 1K85; -.
DR AlphaFoldDB; P20533; -.
DR BMRB; P20533; -.
DR SMR; P20533; -.
DR CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EvolutionaryTrace; P20533; -.
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: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; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.10.50.10; -; 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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS50853; FN3; 2.
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; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..41
FT CHAIN 42..699
FT /note="Chitinase A1"
FT /id="PRO_0000011905"
FT DOMAIN 44..454
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 467..553
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 562..647
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 449..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 135..136
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 162..165
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 205
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 277..280
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 433
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT MUTAGEN 200
FT /note="D->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:8103047"
FT MUTAGEN 200
FT /note="D->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:8103047"
FT MUTAGEN 204
FT /note="E->D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8103047"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1ITX"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 220..242
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:1ITX"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 331..344
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:1ITX"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:1ITX"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1ITX"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 412..425
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1ITX"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:1ITX"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:1K85"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:1K85"
FT STRAND 587..611
FT /evidence="ECO:0007829|PDB:1K85"
FT STRAND 619..628
FT /evidence="ECO:0007829|PDB:1K85"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:1K85"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:1ED7"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:1ED7"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:1ED7"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:1ED7"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:1ED7"
SQ SEQUENCE 699 AA; 73678 MW; AC7C9B22E2987643 CRC64;
MINLNKHTAF KKTAKFFLGL SLLLSVIVPS FALQPATAEA ADSYKIVGYY PSWAAYGRNY
NVADIDPTKV THINYAFADI CWNGIHGNPD PSGPNPVTWT CQNEKSQTIN VPNGTIVLGD
PWIDTGKTFA GDTWDQPIAG NINQLNKLKQ TNPNLKTIIS VGGWTWSNRF SDVAATAATR
EVFANSAVDF LRKYNFDGVD LDWEYPVSGG LDGNSKRPED KQNYTLLLSK IREKLDAAGA
VDGKKYLLTI ASGASATYAA NTELAKIAAI VDWINIMTYD FNGAWQKISA HNAPLNYDPA
ASAAGVPDAN TFNVAAGAQG HLDAGVPAAK LVLGVPFYGR GWDGCAQAGN GQYQTCTGGS
SVGTWEAGSF DFYDLEANYI NKNGYTRYWN DTAKVPYLYN ASNKRFISYD DAESVGYKTA
YIKSKGLGGA MFWELSGDRN KTLQNKLKAD LPTGGTVPPV DTTAPSVPGN ARSTGVTANS
VTLAWNASTD NVGVTGYNVY NGANLATSVT GTTATISGLT AGTSYTFTIK AKDAAGNLSA
ASNAVTVSTT AQPGGDTQAP TAPTNLASTA QTTSSITLSW TASTDNVGVT GYDVYNGTAL
ATTVTGTTAT ISGLAADTSY TFTVKAKDAA GNVSAASNAV SVKTAAETTN PGVSAWQVNT
AYTAGQLVTY NGKTYKCLQP HTSLAGWEPS NVPALWQLQ
