SUS_ACICK
ID SUS_ACICK Reviewed; 793 AA.
AC A0A059ZV61;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Sucrose synthase;
DE Short=SuSyAc {ECO:0000303|PubMed:25846332};
DE EC=2.4.1.13 {ECO:0000269|PubMed:25846332};
GN ORFNames=Acaty_c1477;
OS Acidithiobacillus caldus (strain ATCC 51756 / DSM 8584 / KU).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=637389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51756 / DSM 8584 / KU;
RX PubMed=19617360; DOI=10.1128/jb.00843-09;
RA Valdes J., Quatrini R., Hallberg K., Dopson M., Valenzuela P.D.,
RA Holmes D.S.;
RT "Draft genome sequence of the extremely acidophilic bacterium
RT Acidithiobacillus caldus ATCC 51756 reveals metabolic versatility in the
RT genus Acidithiobacillus.";
RL J. Bacteriol. 191:5877-5878(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 51756 / DSM 8584 / KU;
RX PubMed=25846332; DOI=10.1007/s00253-015-6548-7;
RA Diricks M., De Bruyn F., Van Daele P., Walmagh M., Desmet T.;
RT "Identification of sucrose synthase in nonphotosynthetic bacteria and
RT characterization of the recombinant enzymes.";
RL Appl. Microbiol. Biotechnol. 99:8465-8474(2015).
CC -!- FUNCTION: Catalyzes the reversible conversion of sucrose and a
CC nucleotide disphosphate (NDP) into fructose and NDP-glucose; although
CC the reaction is freely reversible in vitro, the physiological reaction
CC seems to be sucrose cleavage. Unlike characterized plant enzymes
CC prefers ADP as a cosubstrate, whereas plants prefer UDP. The KM for
CC sucrose is 45-fold lower in the presence of ADP than UDP. Its
CC preference for ADP over UDP suggests it may directly link sucrose and
CC glycogen metabolism (Probable). {ECO:0000269|PubMed:25846332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC Evidence={ECO:0000269|PubMed:25846332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-alpha-D-glucose + D-fructose = ADP + H(+) + sucrose;
CC Xref=Rhea:RHEA:55080, ChEBI:CHEBI:15378, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57498, ChEBI:CHEBI:456216;
CC EC=2.4.1.13; Evidence={ECO:0000269|PubMed:25846332};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for ADP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC KM=16.9 mM for CDP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC KM=8.5 mM for GDP in sucrose breakdown {ECO:0000269|PubMed:25846332};
CC KM=7.8 mM for UDP in sucrose breakdown {ECO:0000269|PubMed:25846332};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:25846332};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Remains stable after 15
CC minutes at 60 degrees Celsius. {ECO:0000269|PubMed:25846332};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q820M5}.
CC -!- BIOTECHNOLOGY: Could be used to synthesize NDP-sugars for large-scale
CC glycosylation processes; its comparatively high thermostability would
CC be useful. {ECO:0000305|PubMed:25846332}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 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; CP005986; AIA55343.1; -; Genomic_DNA.
DR RefSeq; WP_004872341.1; NZ_CP005986.1.
DR AlphaFoldDB; A0A059ZV61; -.
DR SMR; A0A059ZV61; -.
DR STRING; 637389.Acaty_c1477; -.
DR EnsemblBacteria; AIA55343; AIA55343; Acaty_c1477.
DR GeneID; 65277037; -.
DR KEGG; acz:Acaty_c1477; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_019158_1_0_6; -.
DR BRENDA; 2.4.1.13; 13376.
DR Proteomes; UP000005522; Chromosome.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR000368; Sucrose_synth.
DR InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR PANTHER; PTHR45839; PTHR45839; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02470; sucr_synth; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..793
FT /note="Sucrose synthase"
FT /id="PRO_0000442255"
FT REGION 263..742
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P49040"
SQ SEQUENCE 793 AA; 91172 MW; 8A3C9E5F5D6B336D CRC64;
MIEALRQQLL DDPRSWYAFL RHLVASQRDS WLYTDLQRAC ADFREQLPEG YAEGIGPLED
FVAHTQEVIF RDPWMVFAWR PRPGRWIYVR IHREQLALEE LSTDAYLQAK EGIVGLGAEG
EAVLTVDFRD FRPVSRRLRD ESTIGDGLTH LNRRLAGRIF SDLAAGRSQI LEFLSLHRLD
GQNLMLSNGN TDFDSLRQTV QYLGTLPRET PWAEIREDMR RRGFAPGWGN TAGRVRETMR
LLMDLLDSPS PAALESFLDR IPMISRILIV SIHGWFAQDK VLGRPDTGGQ VVYILDQARA
LEREMRNRLR QQGVDVEPRI LIATRLIPES DGTTCDQRLE PVVGAENVQI LRVPFRYPDG
RIHPHWISRF KIWPWLERYA QDLEREVLAE LGSRPDLIIG NYSDGNLVAT LLSERLGVTQ
CNIAHALEKS KYLYSDLHWR DHEQDHHFAC QFTADLIAMN AADIIVTSTY QEIAGNDREI
GQYEGHQDYT LPGLYRVENG IDVFDSKFNI VSPGADPRFY FSYARTEERP SFLEPEIESL
LFGREPGADR RGVLEDRQKP LLLSMARMDR IKNLSGLAEL YGRSSRLRGL ANLVIIGGHV
DVGNSRDAEE REEIRRMHEI MDHYQLDGQL RWVGALLDKT VAGELYRVVA DGRGVFVQPA
LFEAFGLTVI EAMSSGLPVF ATRFGGPLEI IEDGVSGFHI DPNDHEATAE RLADFLEAAR
ERPKYWLEIS DAALARVAER YTWERYAERL MTIARIFGFW RFVLDRESQV MERYLQMFRH
LQWRPLAHAV PME
