ID A0A1G4QXS9_9FIRM Unreviewed; 762 AA.
AC A0A1G4QXS9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|ARBA:ARBA00019623, ECO:0000256|RuleBase:RU362110};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758, ECO:0000256|RuleBase:RU362110};
DE AltName: Full=Invertase {ECO:0000256|ARBA:ARBA00033367, ECO:0000256|RuleBase:RU365015};
GN ORFNames=SAMN02910456_01404 {ECO:0000313|EMBL:SCW49228.1};
OS Ruminococcaceae bacterium YRB3002.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520819 {ECO:0000313|EMBL:SCW49228.1, ECO:0000313|Proteomes:UP000199293};
RN [1] {ECO:0000313|EMBL:SCW49228.1, ECO:0000313|Proteomes:UP000199293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YRB3002 {ECO:0000313|EMBL:SCW49228.1,
RC ECO:0000313|Proteomes:UP000199293};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC source. {ECO:0000256|RuleBase:RU365015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000256|RuleBase:RU362110};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|ARBA:ARBA00004914, ECO:0000256|RuleBase:RU365015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR EMBL; FMTG01000008; SCW49228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4QXS9; -.
DR STRING; 1520819.SAMN02910456_01404; -.
DR OrthoDB; 9759709at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000199293; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01167; bac_FRK; 1.
DR CDD; cd18623; GH32_ScrB-like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR006232; Suc6P_hydrolase.
DR NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF00294; PfkB; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000199293};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 9..312
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 390..424
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
FT DOMAIN 440..749
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 762 AA; 84724 MW; 08FE5B7DC18340D8 CRC64;
MTDWKQKLHI EPPQGWLNDP NGLCFCSGKY HVYFQYAPDS ASGGGRKCWG HMESPDLLTW
EYTGIVMEPD IPEDRNGVYS GCAVVDKGKL HIFYTGNVKN PGNYDYINEG REANQIHVVT
DDPKALSGKN IILRNSDYPD YCSCHVRDPK VWIEDGVWKM VLGARTRDSK GLVLYYEGDG
PENFKFVKTY QIPDFGYMWE CPDLFFVDGM SFLGLSPQGL EHEEFRNQNV YSSGYFRIND
EKLCDFEEFD YGFDFYAPQT FEAPDGRRLL IGWMGIGDIP YTNPTVELGW QHCLTLPRQL
TISSDGGIFQ NPIDEILNLR SSRLVYAAGQ KTEIDLPCDI VIKDTGFSRA CFGGLDVTVN
DGIAQLKFDE NYGWGYGRDV RKVRIGDFKN IRIILDTSSV EIYINGGRYV LSSRFYPDKT
VTFECDSQAV IYALGGKPMK LLAIGEALID FIPDKSGCAF DQVTAFAPKL GGAPANVCGA
FSRLTGKSAI LTKLGNDPFG DKIIKELGEA GIDTSDVIRT DEANTALAFV SLGEDGNRTF
SFYRNPSADM LLKDTELSEE VFEDIFALHF CSVSLGDFPM KDAHRAAINF ARAKGAIISF
DPNLRFALWK SEDDLRAAVN EFIPKADILK ISDEEIGFIT GKNDIRDAAE EFFGQGVKLV
VYTRGKDGAE LMTRKASGQT EGIAVKAVDT TGAGDAYIGS LLWYLKSIGV TSADLPELTA
DELKEGAAFA NRYCAVTITK PGAIPSYPTL QNFKKIYKQE DI
//