SUS_NITEU
ID SUS_NITEU Reviewed; 794 AA.
AC Q820M5;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Sucrose synthase;
DE Short=SuSyNe {ECO:0000303|PubMed:25846332};
DE EC=2.4.1.13 {ECO:0000269|PubMed:25846332};
GN Name=ss2; OrderedLocusNames=NE1214;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
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).
RN [3] {ECO:0007744|PDB:4RBN}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF ARG-567; LYS-572 AND GLU-663.
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=26013491; DOI=10.1128/jb.00110-15;
RA Wu R., Asencion Diez M.D., Figueroa C.M., Machtey M., Iglesias A.A.,
RA Ballicora M.A., Liu D.;
RT "The crystal structure of Nitrosomonas europaea sucrose synthase reveals
RT critical conformational changes and insights into sucrose metabolism in
RT prokaryotes.";
RL J. Bacteriol. 197:2734-2746(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
CC (PubMed:25846332, PubMed:26013491). The KM for sucrose is 8-fold lower
CC in the presence of ADP than UDP (PubMed:25846332). Its preference for
CC ADP over UDP suggests it may directly link sucrose and glycogen
CC metabolism (Probable). {ECO:0000269|PubMed:25846332,
CC ECO:0000269|PubMed:26013491, ECO:0000305}.
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, ECO:0000269|PubMed:26013491};
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 ECO:0000269|PubMed:26013491};
CC -!- ACTIVITY REGULATION: Inhibited by GDP over 10 mM and by over 2 mM
CC MgCl(2). {ECO:0000269|PubMed:25846332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 mM for sucrose with ADP during sucrose degradation
CC {ECO:0000269|PubMed:25846332};
CC KM=321 mM for sucrose with UDP during sucrose degradation
CC {ECO:0000269|PubMed:25846332};
CC KM=0.44 mM for ADP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC KM=1.28 mM for CDP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC KM=1.56 mM for GDP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC KM=0.69 mM for UDP in sucrose breakdown
CC {ECO:0000269|PubMed:25846332};
CC Vmax=20.8 umol/min/mg enzyme in sucrose breakdown with ADP
CC {ECO:0000269|PubMed:25846332};
CC Vmax=11.5 umol/min/mg enzyme in sucrose breakdown with CDP
CC {ECO:0000269|PubMed:25846332};
CC Vmax=40.1 umol/min/mg enzyme in sucrose breakdown with GDP
CC {ECO:0000269|PubMed:25846332};
CC Vmax=67.7 umol/min/mg enzyme in sucrose breakdown with UDP
CC {ECO:0000269|PubMed:25846332};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:25846332};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. Retains about 55% activity
CC after 15 minutes at 65 degrees Celsius.
CC {ECO:0000269|PubMed:25846332};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26013491}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; AL954747; CAD85125.1; -; Genomic_DNA.
DR RefSeq; WP_011111802.1; NC_004757.1.
DR PDB; 4RBN; X-ray; 3.05 A; A/B/C/D=1-794.
DR PDBsum; 4RBN; -.
DR AlphaFoldDB; Q820M5; -.
DR SMR; Q820M5; -.
DR STRING; 228410.NE1214; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; CAD85125; CAD85125; NE1214.
DR KEGG; neu:NE1214; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_019158_1_0_4; -.
DR OMA; WISRFEI; -.
DR OrthoDB; 694191at2; -.
DR PhylomeDB; Q820M5; -.
DR BRENDA; 2.4.1.13; 3654.
DR Proteomes; UP000001416; 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 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..794
FT /note="Sucrose synthase"
FT /id="PRO_0000442258"
FT REGION 263..742
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P49040"
FT MUTAGEN 567
FT /note="R->A: 2500-fold decrease in Vmax for UDP-glucose,
FT 2600-fold decrease for ADP-glucose."
FT /evidence="ECO:0000269|PubMed:26013491"
FT MUTAGEN 572
FT /note="K->A: 2200-fold decrease in Vmax for UDP-glucose,
FT 2300-fold decrease for ADP-glucose."
FT /evidence="ECO:0000269|PubMed:26013491"
FT MUTAGEN 663
FT /note="E->A: 430-fold decrease in Vmax for UDP-glucose,
FT 185-fold decrease for ADP-glucose."
FT /evidence="ECO:0000269|PubMed:26013491"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 290..311
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 376..390
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 433..438
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 448..461
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 545..549
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 585..590
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 592..596
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 604..607
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 612..623
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 630..633
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 650..653
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 667..675
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 686..690
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:4RBN"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 708..716
FT /evidence="ECO:0007829|PDB:4RBN"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 725..740
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 743..764
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 766..768
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 769..781
FT /evidence="ECO:0007829|PDB:4RBN"
FT HELIX 783..787
FT /evidence="ECO:0007829|PDB:4RBN"
SQ SEQUENCE 794 AA; 90865 MW; 3A046387F29DF2CB CRC64;
MTTIDTLATC TQQNRDAVYT LLRRYFTANR TLLLQSDLRE GLLQTEQDCG QSDMLRAFVF
RLQEGIFSSP WAYLALRPEI AKWEFMRIHQ EHLIPEKLTI SEFLKFKETV VKGEATESVL
EVDFGPFNRG FPRLKESRSI GQGVIFLNRK LSSEMFSRIE AGHTSLLHFL GVHAIEGQQL
MFSNNSHDIH AVRNQLRQAL EMLETLDGTT PWIELAPKMN QLGFAPGWGH NANRVAETMN
MLMDILEAPS PSALEEFLAC IPMISRLLIL SPHGYFGQDN VLGLPDTGGQ VVYILDQVRA
LEKEMHDRLQ LQGVQVEPKI LIVTRLIPDA GDTTCNQRLE KVSGCTNTWI LRVPFRKHNG
EIIPHWISRF EIWPHLEIFA GDVEREALAE LGGHPDLIIG NYSDGNLVAT LLSRRLGVTQ
CNIAHALEKT KYLHSDIYWQ ENEDKYHFSC QYTADLLAMN SADFIVTSTY QEIAGTREAE
GQYESYQAFS MPDLYRVIHG IDLFDPKFNI VSPGANADIY FPYSDPNRRL HSLIPEIESL
IFDDATNLPA RGYLQDPDKP LIFTMARLDR IKNITGLVEL YAASPRLRSL ANLVIVGGKI
DPQHSSDHEE QEQIHRMHQL MDEHELDQQV RWLGMRLDKN LAGELYRYIA DKRGIFVQPA
LFEAFGLTII EAMASGLPTF ATRYGGPLEI IQNNRSGFHI DPNQGAATAD LIADFFEKNL
ENPQEWERIS QGALDRVASR YTWKLYAERM MTLSRIYGFW KFVSGLEREE TDRYLNMFYH
LQFRPLANRL AHEI
