DEAA_VIBAL
ID DEAA_VIBAL Reviewed; 427 AA.
AC Q99PX1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Chitin disaccharide deacetylase;
DE EC=3.5.1.105 {ECO:0000269|PubMed:16232910};
DE AltName: Full=Chitin oligosaccharide deacetylase;
DE Flags: Precursor;
GN Name=deaA;
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=H-8;
RX PubMed=16232910; DOI=10.1016/s1389-1723(01)80041-4;
RA Ohishi K., Murase K., Ohta T., Etoh H.;
RT "Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus
RT H-8.";
RL J. Biosci. Bioeng. 90:561-563(2000).
CC -!- FUNCTION: Specifically catalyzes the degradation of N,N'-
CC diacetylchitobiose. Key enzyme in the chitin catabolic cascade.
CC {ECO:0000269|PubMed:16232910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,N'-diacetylchitobiose = acetate + N-acetyl-beta-D-
CC glucosaminyl-(1->4)-D-glucosamine; Xref=Rhea:RHEA:27469,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28681, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:59910; EC=3.5.1.105;
CC Evidence={ECO:0000269|PubMed:16232910};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC Carbohydrate-binding module 12 subfamily. {ECO:0000305}.
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DR EMBL; AB055217; BAB21759.1; -; Genomic_DNA.
DR EMBL; AJ292005; CAC29092.1; -; Genomic_DNA.
DR AlphaFoldDB; Q99PX1; -.
DR SMR; Q99PX1; -.
DR STRING; 663.BAU10_12895; -.
DR CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR eggNOG; COG0726; Bacteria.
DR BioCyc; MetaCyc:MON-15495; -.
DR BRENDA; 3.5.1.105; 6624.
DR UniPathway; UPA00349; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004099; F:chitin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF51055; SSF51055; 2.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:16232910"
FT CHAIN 23..427
FT /note="Chitin disaccharide deacetylase"
FT /id="PRO_5000066304"
FT DOMAIN 28..326
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT DOMAIN 333..375
FT /note="Chitin-binding type-3 1"
FT DOMAIN 382..419
FT /note="Chitin-binding type-3 2"
SQ SEQUENCE 427 AA; 47050 MW; 0E6EA65111BD2770 CRC64;
MKLNKLAIAT LVSAALSQYA FAQTDTKGTI YLTFDDGPIN ASIDVINVLN QEEVKATFYF
NAWHLDGIGD ENEDRALEAL KLALDSGHIV ANHSYDHMVH NCVEEFGPNS AAECNATGDH
QINSYQDPAY DASMFAENLS VLEKYLPNIT SYPNYKANEF ARLPYTNGWR VTKDFKADGL
CATSDDLKPW EPGYSCDTAN PSNSVKAAIA VQNILANNGY QTHGWDVDWA PENWGIAMPA
NSLTEAEPFL GYVDSALNTC APTTINPINS KAQEFPCGTP LHADKVIVLT HEFLFEDGKR
GMGATQNLPK LAKFIQLAKQ AGYVFDTMDN YTPNWQVGNN YSAGDYVLHL GTVYQAVTSH
TAQQDWAPSP TSSLWTNADP ATNWTQNVSY KQGDVVTYQG LRYLVNVPHV SQADWTPNSQ
NTLFTAL
