SOPH_PARD8
ID SOPH_PARD8 Reviewed; 721 AA.
AC A6LGF6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end) {ECO:0000305};
DE EC=3.2.1.214 {ECO:0000269|PubMed:29763309};
DE AltName: Full=2-beta-D-glucooligosaccharide sophorohydrolase (non-reducing end) {ECO:0000303|PubMed:29763309};
DE AltName: Full=Beta-1,2-glucanase {ECO:0000303|PubMed:29763309};
DE Flags: Precursor;
GN OrderedLocusNames=BDI_3064 {ECO:0000312|EMBL:ABR44770.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
RN [2] {ECO:0007744|PDB:5Z06}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 19-721, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=29763309; DOI=10.1021/acs.biochem.8b00385;
RA Shimizu H., Nakajima M., Miyanaga A., Takahashi Y., Tanaka N.,
RA Kobayashi K., Sugimoto N., Nakai H., Taguchi H.;
RT "Characterization and structural analysis of a novel exo-type enzyme acting
RT on beta-1,2-glucooligosaccharides from Parabacteroides distasonis.";
RL Biochemistry 57:3849-3860(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of linear beta-1,2-glucan and beta-
CC 1,2-glucooligosaccharides with degrees of polymerization (DPs) greater
CC than or equal to 4, to produce sophorose. The best substrates are
CC tetra- and pentasaccharides. Acts as an exo-type enzyme that releases
CC sophorose from the non-reducing end of the substrate. It cannot
CC hydrolyze cyclic beta-1,2-glucans. {ECO:0000269|PubMed:29763309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->2)-beta-D-glucosyl](n) + H2O = [(1->2)-beta-D-
CC glucosyl](n-2) + sophorose; Xref=Rhea:RHEA:62388, Rhea:RHEA-
CC COMP:11881, Rhea:RHEA-COMP:16082, ChEBI:CHEBI:1230,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:27517; EC=3.2.1.214;
CC Evidence={ECO:0000269|PubMed:29763309};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for beta-1,2-glucotetrasaccharide
CC {ECO:0000269|PubMed:29763309};
CC KM=1.6 mM for beta-1,2-glucopentasaccharide
CC {ECO:0000269|PubMed:29763309};
CC KM=1.0 mM for beta-1,2-glucan (with an average DP of 77)
CC {ECO:0000269|PubMed:29763309};
CC Note=kcat is 54 sec(-1) with beta-1,2-glucotetrasaccharide as
CC substrate. kcat is 29 sec(-1) with beta-1,2-glucopentasaccharide as
CC substrate. kcat is 0.48 sec(-1) with beta-1,2-glucan (with an average
CC DP of 77) as substrate. {ECO:0000269|PubMed:29763309};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:29763309};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:29763309};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29763309}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:29763309}.
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DR EMBL; CP000140; ABR44770.1; -; Genomic_DNA.
DR RefSeq; WP_011967128.1; NC_009615.1.
DR PDB; 5Z06; X-ray; 2.10 A; A/B=19-721.
DR PDBsum; 5Z06; -.
DR SMR; A6LGF6; -.
DR STRING; 435591.BDI_3064; -.
DR EnsemblBacteria; ABR44770; ABR44770; BDI_3064.
DR KEGG; pdi:BDI_3064; -.
DR PATRIC; fig|435591.13.peg.3022; -.
DR eggNOG; COG5368; Bacteria.
DR HOGENOM; CLU_023287_1_0_10; -.
DR OMA; ARINHAY; -.
DR OrthoDB; 1384939at2; -.
DR BioCyc; MetaCyc:MON-21028; -.
DR BioCyc; PDIS435591:G1G5A-3141-MON; -.
DR BRENDA; 3.2.1.214; 754.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR019282; Glycoamylase-like_cons_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF10091; Glycoamylase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..721
FT /note="Exo beta-1,2-glucooligosaccharide sophorohydrolase
FT (non-reducing end)"
FT /id="PRO_5002699300"
FT DOMAIN 474..708
FT /note="Glycoamylase-like"
FT /evidence="ECO:0000255"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 409..425
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 431..445
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 449..453
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 484..492
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 512..522
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 526..529
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 573..590
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5Z06"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 635..639
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 641..653
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:5Z06"
FT TURN 671..674
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 682..697
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 699..705
FT /evidence="ECO:0007829|PDB:5Z06"
FT HELIX 708..719
FT /evidence="ECO:0007829|PDB:5Z06"
SQ SEQUENCE 721 AA; 82568 MW; F6E99D5941DC6523 CRC64;
MKHIALLTTL LLSASLQAVE KPYDYVFFEN SLMKGDYFYS QAKYTSPSWI KNARHHLPVA
GSVAFTPGNS LELTYVSAPG GDWYSEIQYC PVRGNDFFRE PSTLSMQVRL RESMNAAALP
NIAIRYADST YTQYLNLRNY LKDTRPGVWH PVSIPLEDFG LNAVNDTNIK KLAAVALRPG
TADGNEYTIY LDDIELLPAS LPSVSALNAP VLQEAKAYER HIDIKWIPQS KEDIKYYRIY
RSFDGITYQP VAVRRPWMNR YTDFLGEVGK KAYYKVTAVD YALNESNDSQ TVSATTYPMT
DEQLLDMVQE ANFRYYWEGA EPNSGLAREN IPGRNDMIAT GASGFGIMAI VAGIERGFIT
REEGVQRFLK ITSFLEKADK FHGAVSHFID GTTGKTVAFF GPKDNGGDLV ETSFLFQGLL
TARQYFNQEN DKEKQIRKSI DNLWKNVEWS WYKQFKDSPY LYWHWSPDQA WVINHKLIGW
NETMITYMLA IMGPKYGISP EMYYSGWASQ EEYAQEYRAD WGRVEDGKMY TNGNTYYGEN
LKVGVSNGGP LFFIHYSYLG LDPHKFTDKY TNYFENNQKM AKINQRYCIE NQGGYVGYGE
DCWGLTASDF AWNYQAQEPM PHRDNGTMAP TGALASFPYT PDASMKALRN YYRNHGSFLW
GEYGFRDAFN LTVNWVSPLF MGLNQAPVTV MIENYRTNLL WNLFMSHPDV QKGIQKIQSI
K
