ID   SUS_MELRP               Reviewed;         793 AA.
AC   I7A3T6;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Sucrose synthase;
DE            Short=SuSyMr {ECO:0000303|PubMed:25846332};
DE            EC=2.4.1.13 {ECO:0000269|PubMed:25846332};
GN   OrderedLocusNames=MROS_1314;
OS   Melioribacter roseus (strain JCM 17771 / P3M-2).
OC   Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Melioribacter.
OX   NCBI_TaxID=1191523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17771 / P3M-2;
RX   PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA   Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA   Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT   "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT   organotrophic bacterium representing a novel deep lineage within
RT   Bacteriodetes/Chlorobi group.";
RL   PLoS ONE 8:E53047-E53047(2013).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=JCM 17771 / P3M-2;
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 7.0. {ECO:0000269|PubMed:25846332};
CC       Temperature dependence:
CC         Optimum temperature is 80 degrees Celsius. Retains about 40% activity
CC         after 15 minutes at 65 degrees Celsius.
CC         {ECO:0000269|PubMed:25846332};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q820M5}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR   EMBL; CP003557; AFN74551.1; -; Genomic_DNA.
DR   RefSeq; WP_014855986.1; NC_018178.1.
DR   AlphaFoldDB; I7A3T6; -.
DR   SMR; I7A3T6; -.
DR   STRING; 1191523.MROS_1314; -.
DR   EnsemblBacteria; AFN74551; AFN74551; MROS_1314.
DR   KEGG; mro:MROS_1314; -.
DR   PATRIC; fig|1191523.3.peg.1400; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_019158_1_0_10; -.
DR   OMA; WISRFEI; -.
DR   OrthoDB; 694191at2; -.
DR   BRENDA; 2.4.1.13; 14463.
DR   Proteomes; UP000009011; 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..793
FT                   /note="Sucrose synthase"
FT                   /id="PRO_0000442257"
FT   REGION          259..738
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
SQ   SEQUENCE   793 AA;  91768 MW;  AE513C0C9002A3EF CRC64;
     MIKDIYKTAE TFHNDFYDFL KAVSTQPKKL MITGELINLY VASGYDKNSG LYEFIEKIQE
     TISLDHSVIL DVRIKIASIK FYRISLEEFL IEEISSKEFL IYKETVAKPD TLNTTLNLNF
     KPFYDKSPAV RDIKYIGSGV EYLNRFLSSQ MFTNEERWKK NLFDFIRLHN FNGEQLILND
     RIKDTKHLNN QINAALAKLG NHPANTPYEN IKHILQELGF EKGLGKDAGT ITHNLNLLDQ
     LLNSPDHNAL AEFISSIPMI LNIAIISPHG FFGQEGVLGL PDTGGQVVYI LDQVKALEKQ
     LIDSLKKSGL NLLPKIIVLT RLIPNARGTT CNQRLEKIYG AKNSWILRVP FREYNKRVTD
     EWISRFEIWP YLEDFAEDSY TALLAEFKKR PDLIIGNYSD GNLVAYLLAK KFKVTQCGIA
     HALEKSKYLY SALYWYDLEK YYHFSMQFTA DLLAINSADF LITSSFQEIA GTEKSIGQYE
     SYMHFTMPGL YRVENGVNPF HVKFNIVSPG VNEKIYFPYP KTKWRLKETK RRIENLFFSN
     SEDPDVIGWL DNPEKTPIFT MSRLDRIKNI SFLVRCFGES EELQQTSNLI VVAGKIDETM
     TDDYEEKEQI RLMHELITKY KLHNKIRWIG KLLPKDESGE AYRIIAERRG IFVQPALFEG
     FGLTVLEAMT SGLPVFATKY GGPLEIIQNG VNGFHIDPVN QEETTEKIVR FLSDSYIDSS
     VWDKLSKAAI KRVTEKYSWK LYSKRLLSLA KLYGFWKYAT NLEHEDINAY LDLIYHTIYK
     SRAKILLEEH MKR