SQD1_SPIOL
ID SQD1_SPIOL Reviewed; 482 AA.
AC Q84KI6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=UDP-sulfoquinovose synthase, chloroplastic;
DE EC=3.13.1.1;
DE AltName: Full=SoSQD1;
DE AltName: Full=Sulfite:UDP-glucose sulfotransferase;
DE AltName: Full=Sulfolipid biosynthesis protein;
DE Flags: Precursor;
GN Name=SQD1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Melody;
RX PubMed=12706349; DOI=10.1016/s0003-9861(03)00112-7;
RA Shimojima M., Benning C.;
RT "Native uridine 5'-diphosphate-sulfoquinovose synthase, SQD1, from spinach
RT purifies as a 250-kDa complex.";
RL Arch. Biochem. Biophys. 413:123-130(2003).
RN [2]
RP INTERACTION WITH FDGOGAT, AND 3D-STRUCTURE MODELING.
RX PubMed=15752726; DOI=10.1016/j.abb.2005.02.005;
RA Shimojima M., Hoffmann-Benning S., Garavito R.M., Benning C.;
RT "Ferredoxin-dependent glutamate synthase moonlights in plant sulfolipid
RT biosynthesis by forming a complex with SQD1.";
RL Arch. Biochem. Biophys. 436:206-214(2005).
CC -!- FUNCTION: Involved in the biosynthesis of sulfolipids found in
CC thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid
CC head group precursor UDP-sulfoquinovose. The sulfite is delivered to
CC the reaction center by the FMN-binding domain of FdGOGAT.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-
CC sulfoquinovose; Xref=Rhea:RHEA:13197, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:60009; EC=3.13.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for UDP-glucose;
CC KM=5 uM for sulfite;
CC pH dependence:
CC Optimum pH is 8.0-8.5.;
CC -!- SUBUNIT: Homodimer. Interacts with FdGOGAT (via FMN-binding domain).
CC {ECO:0000269|PubMed:15752726}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12706349}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AY192559; AAO39667.1; -; mRNA.
DR AlphaFoldDB; Q84KI6; -.
DR SMR; Q84KI6; -.
DR BRENDA; 3.13.1.1; 5812.
DR GO; GO:0009570; C:chloroplast stroma; IDA:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0101016; F:FMN-binding domain binding; IPI:CAFA.
DR GO; GO:0046507; F:UDPsulfoquinovose synthase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; NAD; Plastid; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..482
FT /note="UDP-sulfoquinovose synthase, chloroplastic"
FT /id="PRO_0000010470"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 100..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 120..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 163..164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 327..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 342..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 415..417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT SITE 274
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:O48917"
SQ SEQUENCE 482 AA; 53811 MW; 157BF49394841960 CRC64;
MAHLLSTSCS MKVSPSEKLS SKCWNIGSTK YPMSFTQQTS KSAFKSLVHQ RNNTQKLTVV
RATTVPLNQE TKAESGTSSF ENNGNTSGRK RVMVIGGDGY CGWATALHLS KKNYDVCIVD
NLVRRLFDHQ LGLDSLTPIA SIQNRIRRWQ GLTGKTIDLH VGDICDFEFL AETFKSFEPD
TVVHFGEQRS APYSMIDRSR AVYTQQNNVI GTINVLFAIK EFSEECHLVK LGTMGEYGTP
NIDIEEGFIT ITHNGRTDTL PYPKQASSFY HLSKVHDSHN IAFTCKAWGI RATDLNQGVV
YGVMTEETAM HEELCNRFDY DAVFGTALNR FCVQAAVGHP LTVYGKGGQT RGYLDIRDTV
QCVELAIANP AKLGEFRVFN QFTEQYSVRD LAALVTKAGE KLGLNVETIS VPNPRVEAEE
HYYNAKHTKL AELGLKPHLL SDSLLDSVLN FAVQYKDRVD TKQIMPSVSW KKIGVKPQTL
RA
