SACB_GLUDI
ID SACB_GLUDI Reviewed; 584 AA.
AC Q43998;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Levansucrase;
DE EC=2.4.1.10;
DE AltName: Full=Beta-D-fructofuranosyl transferase;
DE AltName: Full=Sucrose 6-fructosyl transferase;
DE Flags: Precursor;
GN Name=lsdA;
OS Gluconacetobacter diazotrophicus (Acetobacter diazotrophicus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=33996;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 52-61.
RC STRAIN=SRT4 / CBS 550.94;
RX PubMed=8704949; DOI=10.1099/13500872-142-5-1077;
RA Arrieta J., Hernandez L., Coego A., Suarez V., Balmori E., Menendez C.,
RA Petit-Glatron M.-F., Chambert R., Selman-Housein G.;
RT "Molecular characterization of the levansucrase gene from the endophytic
RT sugarcane bacterium Acetobacter diazotrophicus SRT4.";
RL Microbiology 142:1077-1085(1996).
RN [2]
RP DISULFIDE BOND, AND PYROGLUTAMATE FORMATION AT GLN-31.
RX PubMed=10214721;
RX DOI=10.1002/(sici)1096-9888(199903)34:3<169::aid-jms780>3.0.co;2-4;
RA Betancourt L., Takao T., Hernandez L., Padron G., Shimonishi Y.;
RT "Structural characterization of Acetobacter diazotropicus levansucrase by
RT matrix-assisted laser desorption/ionization mass spectrometry:
RT identification of an N-terminal blocking group and a free-thiol cysteine
RT residue.";
RL J. Mass Spectrom. 34:169-174(1999).
CC -!- FUNCTION: Releases fructooligosaccharides and levan, a high-molecular-
CC mass fructosyl polymer, from sucrose. It acts more as a sucrose
CC hydrolase than as a fructan polymerase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside +
CC sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-
CC glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-
CC COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 68 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; L41732; AAB36606.1; -; Genomic_DNA.
DR RefSeq; WP_012222901.1; NZ_VITL01000003.1.
DR PDB; 1W18; X-ray; 2.50 A; A/B=62-554.
DR PDBsum; 1W18; -.
DR AlphaFoldDB; Q43998; -.
DR SMR; Q43998; -.
DR CAZy; GH68; Glycoside Hydrolase Family 68.
DR OMA; NGWSVIV; -.
DR BRENDA; 2.4.1.10; 2464.
DR BRENDA; 3.2.1.65; 2464.
DR SABIO-RK; Q43998; -.
DR EvolutionaryTrace; Q43998; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050053; F:levansucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0009758; P:carbohydrate utilization; IEA:InterPro.
DR CDD; cd08997; GH68; 1.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR003469; Glyco_hydro_68.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF02435; Glyco_hydro_68; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Glycosyltransferase; Pyrrolidone carboxylic acid; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..51
FT /evidence="ECO:0000269|PubMed:8704949"
FT /id="PRO_0000012245"
FT CHAIN 52..584
FT /note="Levansucrase"
FT /id="PRO_0000012246"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT ACT_SITE 401
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q74K42"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10214721"
FT DISULFID 339..395
FT /evidence="ECO:0000269|PubMed:10214721"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 219..232
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 237..249
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 255..272
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1W18"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:1W18"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 431..443
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:1W18"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:1W18"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 493..503
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:1W18"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:1W18"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1W18"
SQ SEQUENCE 584 AA; 63526 MW; CBFBF4139AD0B8CE CRC64;
MAHVRRKVAT LNMALAGSLL MVLGAQSALA QGNFSRQEAA RMAHRPGVMP RGGPLFPGRS
LAGVPGFPLP SIHTQQAYDP QSDFTARWTR ADALQIKAHS DATVAAGQNS LPAQLTMPNI
PADFPVINPD VWVWDTWTLI DKHADQFSYN GWEVIFCLTA DPNAGYGFDD RHVHARIGFF
YRRAGIPASR RPVNGGWTYG GHLFPDGASA QVYAGQTYTN QAEWSGSSRL MQIHGNTVSV
FYTDVAFNRD ANANNITPPQ AIITQTLGRI HADFNHVWFT GFTAHTPLLQ PDGVLYQNGA
QNEFFNFRDP FTFEDPKHPG VNYMVFEGNT AGQRGVANCT EADLGFRPND PNAETLQEVL
DSGAYYQKAN IGLAIATDST LSKWKFLSPL ISANCVNDQT ERPQVYLHNG KYYIFTISHR
TTFAAGVDGP DGVYGFVGDG IRSDFQPMNY GSGLTMGNPT DLNTAAGTDF DPSPDQNPRA
FQSYSHYVMP GGLVESFIDT VENRRGGTLA PTVRVRIAQN ASAVDLRYGN GGLGGYGDIP
ANRADVNIAG FIQDLFGQPT SGLAAQASTN NAQVLAQVRQ FLNQ
