ID   SUS_DENA2               Reviewed;         786 AA.
AC   D4H6M0;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Sucrose synthase;
DE            Short=SuSyDa {ECO:0000303|PubMed:25846332};
DE            EC=2.4.1.13 {ECO:0000269|PubMed:25846332};
GN   OrderedLocusNames=Dacet_2944;
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460;
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460;
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 (By
CC       similarity). Its preference for ADP over UDP suggests it may directly
CC       link sucrose and glycogen metabolism (Probable).
CC       {ECO:0000250|UniProtKB:A0A059ZV61, 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:25846332};
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius. Very thermounstable,
CC         complete loss of activity after 15 minutes at 60 degrees Celsius.
CC         {ECO:0000269|PubMed:25846332};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q820M5}.
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; CP001968; ADD69694.1; -; Genomic_DNA.
DR   RefSeq; WP_013012179.1; NC_013943.1.
DR   AlphaFoldDB; D4H6M0; -.
DR   SMR; D4H6M0; -.
DR   STRING; 522772.Dacet_2944; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ADD69694; ADD69694; Dacet_2944.
DR   KEGG; dap:Dacet_2944; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_019158_1_0_0; -.
DR   OMA; WISRFEI; -.
DR   OrthoDB; 694191at2; -.
DR   BRENDA; 2.4.1.13; 14462.
DR   Proteomes; UP000002012; 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; Reference proteome; Transferase.
FT   CHAIN           1..786
FT                   /note="Sucrose synthase"
FT                   /id="PRO_0000442256"
FT   REGION          259..736
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
SQ   SEQUENCE   786 AA;  89796 MW;  523BA7EC6BF63014 CRC64;
     MNLSNKELEG LDEIISDHRE DFCPFLGRIE EEDKQFFLSS EMKEMYAGDT VPDFIASLQE
     AVKMPGQIYF ATRASIGEWA FVTVFTDTLD YMEVSPTEYQ EAKEKTVLGE NAAWMPSVDL
     KPFNRDFPKP SSADFIGKGV EFLNRHQSSR IFMNPEKGLK QLLDFLRVHK YDGRQLMLNN
     RIDSVDKLKK ALKKAQALLK NKSDETEWEE VESDMAHLGF EPGWGKKLGY VKEFLALLSD
     ILAAPEPVVL EKFLDRIPMI FSLVVLSPHG FFGQAGVFGK PDTGGQVVYI LDQVKALEHE
     LKSRLDEKGL DITPKILVVT RLIPEAEGTN CDMEEELIRG TDNCHIVRVP FRDESGEVVR
     QWISRFRIWP YLERFSTEAQ NIILSKLQGN PDLIIGNYSD GNLVASLIAQ RLGVTQCTIA
     HALEKTKYLY SDLYWQDNND KYHFACQYTA DLISMNYSDF IITSTYQEIA GTNDSVGQYE
     SYMNYTLPGL YRVVNGIDVF DPKFNVVSPG AAPDIFFSYK SKDRFPEHIE EIESILFEDN
     LEGSRGSLAD PDKPLIFTMA RLDKIKNLTG LVRWFGENEE LRKTANLLVI GGFVDESLSS
     DDEEREQIRI MHSVIDELGL DGSVRWVGAH LGKRMTGEFY RYVADRKGVF VQPALFEAFG
     LTIIEAMSSG LPVFATVYGG PSEIIEDGKS GFTLDPNKGD ECAEKLLEFI QKCQSDPGHW
     IKISDNALKR VEERYNWPLY AKRLMTFARV YGFWKFVTNL EREETVRYLE MLYGMVYRRL
     ADPKEY