CHBP_VIBPR
ID CHBP_VIBPR Reviewed; 801 AA.
AC Q76IQ9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=N,N'-diacetylchitobiose phosphorylase;
DE EC=2.4.1.280;
DE AltName: Full=Chitobiose phosphorylase;
GN Name=chbP;
OS Vibrio proteolyticus (Aeromonas proteolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=13678418; DOI=10.1042/bj20031171;
RA Honda Y., Kitaoka M., Hayashi K.;
RT "Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus:
RT identification of family 36 glycosyltransferase in Vibrio.";
RL Biochem. J. 377:225-232(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CALCIUM;
RP 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE AND N-ACETYL-D-GLUCOSAMINE, AND
RP SUBUNIT.
RX PubMed=15274915; DOI=10.1016/j.str.2004.03.027;
RA Hidaka M., Honda Y., Kitaoka M., Nirasawa S., Hayashi K., Wakagi T.,
RA Shoun H., Fushinobu S.;
RT "Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl
RT transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold.";
RL Structure 12:937-947(2004).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of chitobiose (N,N'-
CC diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and
CC GlcNAc with inversion of the anomeric configuration.
CC {ECO:0000269|PubMed:13678418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N'-diacetylchitobiose + phosphate = N-acetyl-alpha-D-
CC glucosamine 1-phosphate + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:32527, ChEBI:CHEBI:28681, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:506227; EC=2.4.1.280;
CC Evidence={ECO:0000269|PubMed:13678418};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for N,N'-diacetylchitobiose {ECO:0000269|PubMed:13678418};
CC KM=69 mM for alpha-D-glucosyl-(1-4)-2-acetamide-2-deoxy-D-glucose
CC {ECO:0000269|PubMed:13678418};
CC KM=14 mM for N-acetyl-alpha-D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:13678418};
CC KM=0.48 mM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:13678418};
CC pH dependence:
CC Optimum pH is 7.0-7.7. {ECO:0000269|PubMed:13678418};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:13678418};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15274915}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 94 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB096684; BAC87867.1; -; Genomic_DNA.
DR PDB; 1V7V; X-ray; 1.80 A; A=1-801.
DR PDB; 1V7W; X-ray; 1.60 A; A=1-801.
DR PDB; 1V7X; X-ray; 2.00 A; A=1-801.
DR PDBsum; 1V7V; -.
DR PDBsum; 1V7W; -.
DR PDBsum; 1V7X; -.
DR AlphaFoldDB; Q76IQ9; -.
DR SMR; Q76IQ9; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR KEGG; ag:BAC87867; -.
DR BRENDA; 2.4.1.280; 167.
DR SABIO-RK; Q76IQ9; -.
DR EvolutionaryTrace; Q76IQ9; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11755; GH94N_ChBP_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR009342; Carb-bd_put_dom.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR033432; GH36_catalytic.
DR InterPro; IPR037828; GH94N_ChBP.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR010383; Glyco_hydrolase_94.
DR Pfam; PF17167; Glyco_hydro_36; 1.
DR Pfam; PF06165; Glyco_transf_36; 1.
DR SMART; SM01068; CBM_X; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Transferase.
FT CHAIN 1..801
FT /note="N,N'-diacetylchitobiose phosphorylase"
FT /id="PRO_0000424107"
FT ACT_SITE 489
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 527
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 333
FT /ligand="substrate"
FT BINDING 343
FT /ligand="substrate"
FT BINDING 349..350
FT /ligand="substrate"
FT BINDING 490..492
FT /ligand="substrate"
FT BINDING 637
FT /ligand="substrate"
FT BINDING 644
FT /ligand="substrate"
FT BINDING 690
FT /ligand="substrate"
FT BINDING 709..710
FT /ligand="substrate"
FT BINDING 791
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274915"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15274915"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 283..301
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 363..375
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 502..522
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 525..545
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 577..585
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 591..605
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 659..669
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 678..681
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:1V7W"
FT TURN 698..701
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 703..708
FT /evidence="ECO:0007829|PDB:1V7W"
FT HELIX 711..721
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:1V7V"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 745..752
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 755..762
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:1V7W"
FT STRAND 793..800
FT /evidence="ECO:0007829|PDB:1V7W"
SQ SEQUENCE 801 AA; 90361 MW; BB9D864E7FFB6EDC CRC64;
MKYGYFDNDN REYVITRPDV PAPWTNYLGT EKFCTVISHN AGGYSFYNSP EYNRVTKFRP
NATFDRPGHY VYLRDDDSGD YWSISWQPVA KSLDEAQYQI RHGLSYSKFQ CDYNGIHARK
TLFVPKGEDA EIWDVVIKNT SDQVRTISAF SFVEFSFSHI QSDNQNHQMS LYSAGTAYRP
GLIEYDLYYN TDDFEGFYYL ASTFDPDSYD GQRDRFLGLY RDEANPLAVE QGRCSNSAQT
CYNHCGSLHK QFTLQPGEEI RFAYILGIGK GNGERLREHY QDVANIDAAF AAIKAHWDER
CAKFQVKSPN QGLDTMINAW TLYQAETCVV WSRFASFIEV GGRTGLGYRD TAQDAISVPH
ANPEMTRKRI VDLLRGQVKA GYGLHLFDPD WFDPEKEDVA PSKSPTVVPT PSDEDKIHGI
KDTCSDDHLW LIPTICKYVM ETGETSFFDQ MIPYADGGEA SVYEHMKAAL DFSAEYVGQT
GICKGLRADW NDCLNLGGGE SSMVSFLHFW ALQEFIDLAK FLGKDQDVNT YTEMAANVRE
ACETHLWDDE GGWYIRGLTK NGDKIGTAQQ QEGRVHLESN TLAVLSGLAS QERGEQAMDA
VDEHLFSPYG LHLNAPSFST PNDDIGFVTR VYQGVKENGA IFSHPNPWAW VAETKLGRGD
RAMKFYDALN PYNQNDIIEK RIAEPYSYVQ FIMGRDHQDH GRANHPWLTG TSGWAYFAVT
NYILGVQSGF TGLSVDPCIP SDWPGFEVTR QWRGATYHIQ VENPDHVSKG VKSITLNGAP
IQGRIPPQAQ GSDNQVVVVL G
