OL4AG_CELJU
ID OL4AG_CELJU Reviewed; 816 AA.
AC B3PEE6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Oligosaccharide 4-alpha-D-glucosyltransferase {ECO:0000305};
DE EC=2.4.1.161 {ECO:0000269|PubMed:23132856};
DE AltName: Full=Alpha-glucosidase 31B {ECO:0000305};
DE Short=CJAgd31B {ECO:0000303|PubMed:23132856};
DE Flags: Precursor;
GN Name=agd31B {ECO:0000303|PubMed:23132856};
GN OrderedLocusNames=CJA_3248 {ECO:0000312|EMBL:ACE84782.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000312|EMBL:ACE84782.1};
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ALPHA-ACARBOSE,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23132856; DOI=10.1074/jbc.m112.416511;
RA Larsbrink J., Izumi A., Hemsworth G.R., Davies G.J., Brumer H.;
RT "Structural enzymology of Cellvibrio japonicus Agd31B protein reveals
RT alpha-transglucosylase activity in glycoside hydrolase family 31.";
RL J. Biol. Chem. 287:43288-43299(2012).
CC -!- FUNCTION: Alpha-transglucosylase that specifically transfers single
CC glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-
CC OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl
CC residues. Acts on amylose, amylopectin, glycogen and
CC maltooligosaccharides, with the highest activity with maltotriose as a
CC donor, and also accepts maltose. Does not act as a hydrolase: weak
CC hydrolysis activity is only observed on the disaccharide maltose.
CC {ECO:0000269|PubMed:23132856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers the non-reducing terminal alpha-D-glucose residue
CC from a (1->4)-alpha-D-glucan to the 4-position of a free glucose or
CC of a glucosyl residue at the non-reducing terminus of a (1->4)-alpha-
CC D-glucan, thus bringing about the rearrangement of oligosaccharides.;
CC EC=2.4.1.161; Evidence={ECO:0000269|PubMed:23132856};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.8 mM for maltose {ECO:0000269|PubMed:23132856};
CC KM=1.2 mM for maltotriose {ECO:0000269|PubMed:23132856};
CC KM=1.7 mM for maltotetraose {ECO:0000269|PubMed:23132856};
CC KM=3.1 mM for maltopentaose {ECO:0000269|PubMed:23132856};
CC Note=kcat is 341 sec(-1) for maltose. kcat is 239 sec(-1) for
CC maltotriose. kcat is 123 sec(-1) for maltotetraose. kcat is 181 sec(-
CC 1) for maltopentaose. {ECO:0000269|PubMed:23132856};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; CP000934; ACE84782.1; -; Genomic_DNA.
DR RefSeq; WP_012488824.1; NC_010995.1.
DR PDB; 4B9Y; X-ray; 1.90 A; A=1-816.
DR PDB; 4B9Z; X-ray; 2.00 A; A=1-816.
DR PDB; 4BA0; X-ray; 1.85 A; A=1-816.
DR PDB; 5I23; X-ray; 1.95 A; A=25-816.
DR PDB; 5I24; X-ray; 1.85 A; A=25-816.
DR PDB; 5NPB; X-ray; 1.90 A; A=25-816.
DR PDB; 5NPC; X-ray; 1.96 A; A=25-816.
DR PDB; 5NPD; X-ray; 1.95 A; A=25-816.
DR PDB; 5NPE; X-ray; 1.95 A; A=25-816.
DR PDBsum; 4B9Y; -.
DR PDBsum; 4B9Z; -.
DR PDBsum; 4BA0; -.
DR PDBsum; 5I23; -.
DR PDBsum; 5I24; -.
DR PDBsum; 5NPB; -.
DR PDBsum; 5NPC; -.
DR PDBsum; 5NPD; -.
DR PDBsum; 5NPE; -.
DR AlphaFoldDB; B3PEE6; -.
DR SMR; B3PEE6; -.
DR STRING; 498211.CJA_3248; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PRIDE; B3PEE6; -.
DR EnsemblBacteria; ACE84782; ACE84782; CJA_3248.
DR KEGG; cja:CJA_3248; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_000631_7_2_6; -.
DR OMA; GWPLLRM; -.
DR OrthoDB; 469334at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0033825; F:oligosaccharide 4-alpha-D-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR032513; AGL_N.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF16338; DUF4968; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..816
FT /note="Oligosaccharide 4-alpha-D-glucosyltransferase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430700"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:23132856"
FT ACT_SITE 415
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT BINDING 299
FT /ligand="acarbose"
FT /ligand_id="ChEBI:CHEBI:84363"
FT /evidence="ECO:0000269|PubMed:23132856"
FT BINDING 417
FT /ligand="acarbose"
FT /ligand_id="ChEBI:CHEBI:84363"
FT /evidence="ECO:0000269|PubMed:23132856"
FT BINDING 463
FT /ligand="acarbose"
FT /ligand_id="ChEBI:CHEBI:84363"
FT /evidence="ECO:0000269|PubMed:23132856"
FT BINDING 480
FT /ligand="acarbose"
FT /ligand_id="ChEBI:CHEBI:84363"
FT /evidence="ECO:0000269|PubMed:23132856"
FT BINDING 540
FT /ligand="acarbose"
FT /ligand_id="ChEBI:CHEBI:84363"
FT /evidence="ECO:0000269|PubMed:23132856"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 388..404
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 437..452
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 521..532
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 554..569
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 634..639
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 687..694
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 700..708
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 714..720
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 722..731
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 733..744
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 752..761
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:4BA0"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 790..794
FT /evidence="ECO:0007829|PDB:4BA0"
FT TURN 795..798
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 799..806
FT /evidence="ECO:0007829|PDB:4BA0"
FT STRAND 811..816
FT /evidence="ECO:0007829|PDB:4BA0"
SQ SEQUENCE 816 AA; 92279 MW; 46C43AEBC564851B CRC64;
MFRRIAGFSP IFLMLFGSSL PTMGNPVKRE IHPDAVFYKE HKLRNDGLVI TTNQGNIRLQ
FKSEAAIEVL YRADSKQLPS FALAQPESAI KAQLTETENH LQFSGGTLTA RIQKRPFAIS
YYRDSELLLA EESGFQVNTD KINFRFYLSP GEKILGGGQR ILGMDRRGQR FPLYNRAHYG
YSDHSGQMYF GLPAIMSSKQ YILVFDNSAS GAMDIGKTES DILQLEAKSG RSAYILVAGN
SYPSLIENFT QVTGRQPLPP RWALGSFASR FGYRSEAETR ATVQKYKTED FPLDTIVLDL
YWFGKDIKGH MGNLDWDKEN FPTPLDMMAD FKQQGVKTVL ITEPFVLTSS KRWDDAVKAK
ALAKDPQGQP KAFELYFGNG GIIDVFSKEG SRWFSSIYKD LSKQGVAGWW GDLGEPEMHP
EDTQHAIGDA DTVHNAYGHR WAEMLYQQQL DQFPELRPFI MMRAGFVGSQ RYGMIPWTGD
VSRTWGGLAS QVELALQMSL LGFGYIHSDL GGFADGETLD KEMYIRWLQY GVFQPVYRPH
GQDHIPSEPV FQDEETKAIL RPLVKLRYRM LPYIYTAAYQ NTLTGMPLMR PLFFSDEKNP
ALIDNKTSYF WGDSLLVTPI TQAGVESVSI PAPKGVWFDF WKDTRYQTDG APLTLPTDLH
TIPVLVKAGA FMPYVPAVST TEDYRSDSLE IHYYADASVP LAQGEIFEDD GKDPNSIKRN
QFDLLTLQAT HTDNQLHFQL ARTGKGYRGM PERRATTLVI HNASDQYQHL DINGKTIAIA
QADCASTPAL ACYDQERRQL QLVFTWGREA LNLRLH
