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 04-NOV-2026, entry version 91. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Cellvibrionales; 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 IN COMPLEX WITH ALPHA-ACARBOSE, FUNCTION, CATALYTIC RP ACTIVITY, ACTIVE SITE, AND BIOPHYSICOCHEMICAL 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 CC sec(-1) for maltopentaose. {ECO:0000269|PubMed:23132856}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 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; 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 PDB; 7P4C; X-ray; 1.86 A; AAA=25-816. DR PDB; 7P4D; X-ray; 1.85 A; AAA=25-816. DR PDB; 8RW3; X-ray; 1.90 A; A/B/C=1-816. DR AlphaFoldDB; B3PEE6; -. DR MDposit; B3PEE6; -. DR MDRepo; B3PEE6; -. DR SMR; B3PEE6; -. DR STRING; 498211.CJA_3248; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR KEGG; cja:CJA_3248; -. DR eggNOG; COG1501; Bacteria. DR HOGENOM; CLU_000631_7_2_6; -. DR OMA; AAAQWYK; -. DR OrthoDB; 176168at2; -. DR EvolutionaryTrace; B3PEE6; -. 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 CDD; cd14752; GH31_N; 1. DR CDD; cd06598; GH31_transferase_CtsZ; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR048395; Glyco_hydro_31_C. DR InterPro; IPR025887; Glyco_hydro_31_N_dom. DR InterPro; IPR000322; Glyco_hydro_31_TIM. DR InterPro; IPR013780; Glyco_hydro_b. DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1. DR PANTHER; PTHR22762:SF120; HETEROGLYCAN GLUCOSIDASE 1; 1. DR Pfam; PF13802; Gal_mutarotas_2; 1. DR Pfam; PF01055; Glyco_hydro_31_2nd; 1. DR Pfam; PF21365; Glyco_hydro_31_3rd; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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 255..260 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 //