CHBP_VIBFU
ID CHBP_VIBFU Reviewed; 800 AA.
AC Q9F8X1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=N,N'-diacetylchitobiose phosphorylase;
DE EC=2.4.1.280;
DE AltName: Full=Chitobiose phosphorylase;
GN Name=chbP;
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 1-10, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=10913116; DOI=10.1074/jbc.m001042200;
RA Park J.K., Keyhani N.O., Roseman S.;
RT "Chitin catabolism in the marine bacterium Vibrio furnissii.
RT Identification, molecular cloning, and characterization of A N, N'-
RT diacetylchitobiose phosphorylase.";
RL J. Biol. Chem. 275:33077-33083(2000).
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:10913116}.
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:10913116};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for N,N'-diacetylchitobiose {ECO:0000269|PubMed:10913116};
CC KM=0.51 mM for phosphate {ECO:0000269|PubMed:10913116};
CC Vmax=4.6 nmol/min/ug enzyme with N,N'-diacetylchitobiose as substrate
CC {ECO:0000269|PubMed:10913116};
CC Vmax=4.8 nmol/min/ug enzyme with phosphate as substrate
CC {ECO:0000269|PubMed:10913116};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:10913116};
CC Temperature dependence:
CC Optimum temperature is 20-37 degrees Celsius.
CC {ECO:0000269|PubMed:10913116};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 94 family. {ECO:0000305}.
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DR EMBL; AF230379; AAG23740.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F8X1; -.
DR SMR; Q9F8X1; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR KEGG; ag:AAG23740; -.
DR BioCyc; MetaCyc:MON-16878; -.
DR BRENDA; 2.4.1.280; 6631.
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 Calcium; Direct protein sequencing; Metal-binding; Transferase.
FT CHAIN 1..800
FT /note="N,N'-diacetylchitobiose phosphorylase"
FT /id="PRO_0000424108"
FT ACT_SITE 489
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 490..492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 637
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 644
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 709..710
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 790
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 792
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 800 AA; 89667 MW; 6775D823C051122A CRC64;
MKYGYFDNDN REYVITRPDV PAPWTNYLGT EKFCTVISHN AGGYSFYHSP EYNRVTKFRP
NFTQDRPGHY IYLRDDETGD FWSVSWQPVA KNLDDAHYEV RHGLSYSKFR CDYNGIVATK
TLFVPKGEDA QVWDVEIENT SDQPRTISAF GYVEFSFSHI ASDNQNHQMS LYSAGTEYNN
GVLEYDLYYN TDDFLGFYYL TATFDADSYD GQRDAFLGMY RDEANPIAVA NGRCSNSAQT
CYNHCGALHK QFVLQPGEKV RFAVILGVGK GNGEKLRAKY QDLSQVDAAF AGIKQHWDER
CAKFQVRSPN QGLDTMINAW TLYQAETCVV WSRFASFIEV GGRTGLGYRD TAQDAISVPH
TNPAMTRKRL VDLLRGQVKA GYGLHLFDPD WFDPEKADVK PSKSPTVVPT PSDEDKIHGI
KDTCSDDHLW IVPTILNFVK ETGDLSFIDE VIPYADGGDA TVYQHMMAAL DFSAEYVGQT
GICKGLRADW NDCLNLGGGE SAMVSFLHFW ALEAFLELAR HRQDAAAIDK YQAMANGVRE
ACETHLWDDN GGWYIRGLTK DGDKIGTFEQ QEGKVHLESN TLAVLSGAVS QQRGEKAMDA
VYEYLFSPYG LHLNAPSFAT PNDDIGFVTR VYQGVKENGA IFSHPNPWAW VAEAKLGRGD
RAMEFYDSLN PYNQNDIIET RVAEPYSYVQ FIMGRDHQDH GRANHPWLTG TSGWAYYATT
NFILGVRTGF DTLTVDPCIP AAWSGFEVTR EWRGATYHIS VQNPNGVSKG VQSILVNGEA
VDAINAQPAG SENQVTVILG
