CHB_SERMA
ID CHB_SERMA Reviewed; 885 AA.
AC Q54468;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chitobiase;
DE EC=3.2.1.52;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE Flags: Precursor;
GN Name=chb;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8621090; DOI=10.1016/0378-1119(95)00848-9;
RA Tews I., Vincentelli R., Vorgias C.E.;
RT "N-acetylglucosaminidase (chitobiase) from Serratia marcescens: gene
RT sequence, and protein production and purification in Escherichia coli.";
RL Gene 170:63-67(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=8673609; DOI=10.1038/nsb0796-638;
RA Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E.;
RT "Bacterial chitobiase structure provides insight into catalytic mechanism
RT and the basis of Tay-Sachs disease.";
RL Nat. Struct. Biol. 3:638-648(1996).
CC -!- FUNCTION: Digests the beta-1,4-glycosidic bonds in N-acetylglucosamine
CC (GlcNAc) oligomers (mainly dimers).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; L43594; AAB03808.1; -; Genomic_DNA.
DR PIR; JC4732; JC4732.
DR PDB; 1C7S; X-ray; 1.80 A; A=28-885.
DR PDB; 1C7T; X-ray; 1.90 A; A=28-885.
DR PDB; 1QBA; X-ray; 1.85 A; A=28-885.
DR PDB; 1QBB; X-ray; 2.00 A; A=28-885.
DR PDBsum; 1C7S; -.
DR PDBsum; 1C7T; -.
DR PDBsum; 1QBA; -.
DR PDBsum; 1QBB; -.
DR AlphaFoldDB; Q54468; -.
DR SMR; Q54468; -.
DR STRING; 273526.SMDB11_0477; -.
DR DrugBank; DB03013; N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosamine.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR PRIDE; Q54468; -.
DR BioCyc; MetaCyc:MON-17688; -.
DR UniPathway; UPA00349; -.
DR EvolutionaryTrace; Q54468; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; 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 CDD; cd02847; E_set_Chitobiase_C; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004866; CHB/HEX_N_dom.
DR InterPro; IPR004867; CHB_C_dom.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF03173; CHB_HEX; 1.
DR Pfam; PF03174; CHB_HEX_C; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM01081; CHB_HEX; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Periplasm; Polysaccharide degradation; Signal.
FT SIGNAL 1..27
FT CHAIN 28..885
FT /note="Chitobiase"
FT /id="PRO_0000012018"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="Proton donor"
FT DISULFID 56..66
FT DISULFID 400..408
FT DISULFID 505..578
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1QBA"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 354..366
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 442..452
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 454..469
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 507..526
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:1QBA"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 576..583
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 593..607
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1C7T"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 629..638
FT /evidence="ECO:0007829|PDB:1C7S"
FT TURN 642..645
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 692..697
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:1C7T"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:1QBA"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 744..751
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 754..763
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 777..779
FT /evidence="ECO:0007829|PDB:1QBA"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 788..804
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 806..812
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 823..827
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 830..834
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 840..847
FT /evidence="ECO:0007829|PDB:1C7S"
FT HELIX 857..859
FT /evidence="ECO:0007829|PDB:1C7S"
FT STRAND 868..872
FT /evidence="ECO:0007829|PDB:1C7S"
SQ SEQUENCE 885 AA; 98548 MW; A749CC0F507DE2E1 CRC64;
MNAFKLSALA RLTATMGFLG GMGSAMADQQ LVDQLSQLKL NVKMLDNRAG ENGVDCAALG
ADWASCNRVL FTLSNDGQAI DGKDWVIYFH SPRQTLRVDN DQFKIAHLTG DLYKLEPTAK
FSGFPAGKAV EIPVVAEYWQ LFRNDFLPRW YATSGDAKPK MLANTDTENL DQFVAPFTGD
QWKRTKDDKN ILMTPASRFV SNADLQTLPA GALRGKIVPT PMQVKVHAQD ADLRKGVALD
LSTLVKPAAD VVSQRFALLG VPVQTNGYPI KTDIQPGKFK GAMAVSGAYE LKIGKKEAQV
IGFDQAGVFY GLQSILSLVP SDGSGKIATL DASDAPRFPY RGIFLDVARN FHKKDAVLRL
LDQMAAYKLN KFHFHLSDDE GWRIEIPGLP ELTEVGGQRC HDLSETTCLL PQYGQGPDVY
GGFFSRQDYI DIIKYAQARQ IEVIPEIDMP AHARAAVVSM EARYKKLHAA GKEQEANEFR
LVDPTDTSNT TSVQFFNRQS YLNPCLDSSQ RFVDKVIGEI AQMHKEAGQP IKTWHFGGDE
AKNIRLGAGY TDKAKPEPGK GIIDQSNEDK PWAKSQVCQT MIKEGKVADM EHLPSYFGQE
VSKLVKAHGI DRMQAWQDGL KDAESSKAFA TSRVGVNFWD TLYWGGFDSV NDWANKGYEV
VVSNPDYVYM DFPYEVNPDE RGYYWGTRFS DERKVFSFAP DNMPQNAETS VDRDGNHFNA
KSDKPWPGAY GLSAQLWSET QRTDPQMEYM IFPRALSVAE RSWHRAGWEQ DYRAGREYKG
GETHFVDTQA LEKDWLRFAN ILGQRELAKL DKGGVAYRLP VPGARVAAGK LEANIALPGL
GIEYSTDGGK QWQRYDAKAK PAVSGEVQVR SVSPDGKRYS RAEKV
