ID   CHID_VIBFU              Reviewed;        1046 AA.
AC   P96156;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Chitodextrinase {ECO:0000303|PubMed:8969204};
DE            EC=3.2.1.202 {ECO:0000269|PubMed:8969204};
DE   AltName: Full=Endo-chitodextinase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=endo I;
OS   Vibrio furnissii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=29494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-51, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=8969204; DOI=10.1074/jbc.271.52.33414;
RA   Keyhani N.O., Roseman S.;
RT   "The chitin catabolic cascade in the marine bacterium Vibrio furnissii.
RT   Molecular cloning, isolation, and characterization of a periplasmic
RT   chitodextrinase.";
RL   J. Biol. Chem. 271:33414-33424(1996).
CC   -!- FUNCTION: Hydrolyzes chitin oligosaccharides; (GlcNAc)4 to (GlcNAc)2
CC       and (GlcNAc)5,6 to (GlcNAc)2 and (GlcNAc)3. Inactive towards chitin,
CC       glucosamine oligosaccharides, glycoproteins and glycopeptides
CC       containing (GlcNAc)2. {ECO:0000269|PubMed:8969204}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of chitodextrins, releasing N,N'-diacetylchitobiose
CC         and small amounts of N,N',N''-triacetylchitotriose.; EC=3.2.1.202;
CC         Evidence={ECO:0000269|PubMed:8969204};
CC   -!- ACTIVITY REGULATION: Inhibited by (GlcNAc)4, (GlcNAc)5, (GlcNAc)6, and
CC       PNP-(GlcNAc)3. {ECO:0000269|PubMed:8969204}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:8969204};
CC       Temperature dependence:
CC         Optimum temperature is 35-37 degrees Celsius.
CC         {ECO:0000269|PubMed:8969204};
CC   -!- PATHWAY: Glycan degradation; chitin degradation.
CC       {ECO:0000305|PubMed:8969204}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:8969204}.
CC   -!- INDUCTION: By (GlcNAc)2. {ECO:0000269|PubMed:8969204}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR   EMBL; U41418; AAC44673.1; -; Genomic_DNA.
DR   PIR; T30199; T30199.
DR   AlphaFoldDB; P96156; -.
DR   SMR; P96156; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   BioCyc; MetaCyc:MON-16843; -.
DR   BRENDA; 3.2.1.202; 6631.
DR   UniPathway; UPA00349; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; IPR009470; Chi_C.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF06483; ChiC; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51055; SSF51055; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF54556; SSF54556; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Periplasm; Polysaccharide degradation; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:8969204"
FT   CHAIN           31..1046
FT                   /note="Chitodextrinase"
FT                   /id="PRO_0000011959"
FT   DOMAIN          320..801
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          973..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  112380 MW;  40680F1642D55A1F CRC64;
     MRLHRAKVSK SVFTLSTLTA SCLMAFNSYA AVDCSALAEW QSDTIYTGGD QVQYNGSAYQ
     ANYWTQNNDP EQFSGDYAQW KLLDACTTDG GDDNQAPNAT LTSPSASDVL TTGDVVTLAA
     SASDNDGTIA RVDFLVDGVV VAQASSAPYS ATWTAVAGTH QISAIAYDDK ALASTASQVS
     VSVTDSTQPG NEAPTVDITL SASQVDVGDV VTLTANAADA DGSVDKVDFY VAGSLVGTVA
     STPYTLDYTT TRSGRWLCLR ARLITSARQR IRPRRRLTVA AGPWSVPVVL MVCIKPKGQC
     AVLYGVREDG REKMGADHPR RVIGYFTSWR AGDDDQTAYL VKDIPWEQLT HINYAFVSIG
     SDGKVNVGDV NDANNAAVGK EWDGVEIDPT LGFKGHFGAL ATYKQKYGVK TLISIGGWAE
     TGGHFDNDGN RVADGGFYTM TTNADGSINQ QGIETFADSA VEMMRKYRFD GLDIDLRISN
     IDGGTGNPDD TAFSESRRAY LMNSYHELMR VLREKLDVAS AQDGVHYMLT IAAPSSAYLL
     RGMETMAVTQ YLDYVNIMSY DLHGAWNDHV GHNAALYDTG KDSELAQWNV YGTAQYGGIG
     YLNTDWAFHY FRGSMPAGRI NIGVPYYTRG WQGVTGGDNG LWGARLAKSK RVSNRYGEGE
     KNNCGYGATG LDNMWHDVNA AGDEMGAGSN PMWHAKNLEH GIWGSYLAVY GLDPTTAPLV
     GTYARNYDSV AIAPWLWNAE KKVFLSTEDK QSIDVKADYV IDKEIGGIMF WELAGDYNCY
     VLDANGQRTS IDSTEQACES GQGEYHMGNT MTKAIYDKFK AATPYGNTVA TGAVPSETVD
     IAVSIGGFKV GDQNYPINPK VTFTNNTGVD IPGGTAFQFD IPVSAPDNAK DQSGGGLSVI
     ASGHTRADNI GGLDGTMHRV AFSLPAWKTL PAGDTYELDM VYYLPISGPA NYSVNINGVD
     YAFKFEQPDL PLADLSSGNG GGTGGGDTGG GTTEPGDVVE WVPGSTQVSD GTTVTYNGKC
     FVAQNSPGVW ESPTQTNWFW EEVTCP