KEGG   ENZYME: 3.13.1.1Help
Entry
EC 3.13.1.1                 Enzyme                                 

Name
UDP-sulfoquinovose synthase;
sulfite:UDP-glucose sulfotransferase;
UDPsulfoquinovose synthase;
UDP-6-sulfo-6-deoxyglucose sulfohydrolase
Class
Hydrolases;
Acting on carbon-sulfur bonds;
Acting on carbon-sulfur bonds (only sub-subclass identified to date)
BRITE hierarchy
Sysname
UDP-6-sulfo-6-deoxy-alpha-D-glucose sulfohydrolase
Reaction(IUBMB)
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite [RN:R05775]
Reaction(KEGG)
Substrate
UDP-alpha-D-sulfoquinovopyranose;
H2O [CPD:C00001]
Product
UDP-alpha-D-glucose [CPD:C00029];
sulfite [CPD:C00094]
Comment
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
History
EC 3.13.1.1 created 2001, modified 2010
Pathway
ec00520  Amino sugar and nucleotide sugar metabolism
ec00561  Glycerolipid metabolism
Orthology
K06118  UDP-sulfoquinovose synthase
Genes
ATH: AT4G33030(SQD1)
ALY: ARALYDRAFT_491388
CRB: 17878819
CSAT: 104704938 104716862 104721515 104729959
EUS: EUTSA_v10025085mg
BRP: 103850131 103862211
BNA: 106364202 106368764 106410744 106423381
BOE: 106306811 106306866
THJ: 104818573
CPAP: 110822050
CIT: 102623436
TCC: 18588070
GRA: 105768936
EGR: 104436309
VRA: 106752582
VAR: 108323296
CAM: 101514545
LJA: Lj1g3v4192290.1(Lj1g3v4192290.1) Lj1g3v4202330.1(Lj1g3v4202330.1)
ADU: 107474363
AIP: 107625319
LANG: 109334393
FVE: 101311063
PPER: 18790466
PMUM: 103320566
PAVI: 110765169
MDM: 103455819
PXB: 103952180
ZJU: 107420041
CSV: 101208634
CMO: 103493661
MCHA: 111006075
CMAX: 111481211
CMOS: 111446336
CPEP: 111788170
RCU: 8259571
JCU: 105638141
HBR: 110631761
POP: 7470695
JRE: 109020494
VVI: 100242408
SLY: 100301938(SQD1)
SPEN: 107028543
SOT: 102597858
CANN: 107838884
NSY: 104248240
NTO: 104092521
INI: 109185020
SIND: 105176996
HAN: 110865087
LSV: 111917235
DCR: 108205104
BVG: 104886625
SOE: 110793408
NNU: 104593467
OSA: 4338660
DOSA: Os05t0387200-01(Os05g0387200)
OBR: 102713186
ATS: 109768655(LOC109768655)
SBI: 8077955
ZMA: 100282424
SITA: 101770658
PDA: 103718107
EGU: 105034144
MUS: 104000603
DCT: 110093137
AOF: 109842717
ATR: 18427061
PPP: 112287615
CRE: CHLREDRAFT_27658(SQD1)
APRO: F751_4044
PTI: PHATR_21201(SQD1)
FCY: FRACYDRAFT_268690(SQD1_1)
TPS: THAPSDRAFT_269393(SQDB1)
EHX: EMIHUDRAFT_466230(SQD1)
LOK: Loa_00052
TIG: THII_3662
NOC: Noc_1509
TGR: Tgr7_2097
PPRF: DPRO_3854
DBR: Deba_0024
MES: Meso_2128
SMX: SM11_chr2909(sqdB)
SMI: BN406_02602(SQD1)
SMEL: SM2011_c03961(sqdB)
SMER: DU99_15200
SMD: Smed_2633
RHI: NGR_c27870(sqdB)
SFH: SFHH103_02799(sqdB)
SFD: USDA257_c52080(sqdB)
SAME: SAMCFNEI73_Ch3159(sqdB)
EAD: OV14_0221(sqdB)
ARA: Arad_3686(sqdB)
RET: RHE_CH03468(sqdB)
REC: RHECIAT_CH0003707(sqdB)
RLE: RL3975(sqdB)
RLG: Rleg_3501
RHL: LPU83_3434(sqdB)
RHT: NT26_2661(SQD)
PHL: KKY_937
MMED: Mame_02418(galE_3)
PZU: PHZ_c2966
RSP: RSP_2569(sqdB)
PDE: Pden_2811
KVU: EIO_0713
KVL: KVU_0257(wcaG)
KRO: BVG79_00513(sqdB)
OTM: OSB_26310
MALG: MALG_04603
RSU: NHU_01930
RHC: RGUI_0249
RCE: RC1_2302
HHD: HBHAL_3171(sqdB)
PMW: B2K_20870
AAD: TC41_1261(sqd1)
JEO: JMA_33220
CPAS: Clopa_0781
SAY: TPY_0741(sqd1)
MMC: Mmcs_4564
MKM: Mkms_4652
MJL: Mjls_4947
MVA: Mvan_5143
CAR: cauri_0862(sqdB)
CSX: CSING_04825(SQD1)
CUT: CUTER_03625(sqdB)
CSP: WM42_0503
CAMG: CAMM_09220
CMIN: NCTC10288_01666(sqdB)
NCY: NOCYR_2478(sqd)
RER: RER_49950
ROP: ROP_43120
SERJ: SGUI_2753
PFR: PFREUD_00050(sqdB)
PFRE: RM25_0005
ACE: Acel_0444
SEN: SACE_5690
AMD: AMED_4980(qdb)
AMN: RAM_25350
AMM: AMES_4921(qdb)
AMZ: B737_4921(qdb)
CAI: Caci_6269
RXY: Rxyl_1240
AFO: Afer_0462
SYN: slr1020(sqdB)
SYZ: MYO_15850(sqdB)
SYY: SYNGTS_0579(sqdB)
SYT: SYNGTI_0579(sqdB)
SYS: SYNPCCN_0579(sqdB)
SYQ: SYNPCCP_0579(sqdB)
SYJ: D082_07080(sqdB)
SYW: SYNW0052(sqdB)
SYC: syc0945_c(sqdB)
SYG: sync_0053(sqdB)
SYP: SYNPCC7002_A0847(wcaG)
CYA: CYA_0577
CYB: CYB_0060
SYNR: KR49_09180
SYND: KR52_02210
SYH: Syncc8109_0057(sqdB)
TEL: tll0398
THN: NK55_09000(sqdB)
CYI: CBM981_2369(sqdB)
LET: O77CONTIG1_03860(rfbB)
HHG: XM38_039220(galE)
PMM: PMM1665(sqdB)
PMT: PMT_0050
PMB: A9601_18741(sqdB)
PMC: P9515_18551(sqdB)
PMF: P9303_00511(sqdB)
PMG: P9301_18551(sqdB)
PMH: P9215_19381(sqdB)
PMJ: P9211_17921(sqdB)
PME: NATL1_21351(sqdB)
PRC: EW14_2033
PRM: EW15_2220
AMR: AM1_2812
MAR: MAE_49250
MPK: VL20_3588
CYL: AA637_13670(sqdB)
CHON: NIES4102_14300(wcaG_2)
CYT: cce_4571(sqdB)
TER: Tery_0398
ARP: NIES39_A06480(sqdB)
ANA: alr1744
AVA: Ava_0293
NAZ: Aazo_3746
CALH: IJ00_20580
NSP: BMF81_01595(sqdB)
CTHE: Chro_4417
CEO: ETSB_1310(sqdB)
RCA: Rcas_0045
TRA: Trad_1947
ACA: ACP_1361
ABAS: ACPOL_3980
LOKI: Lokiarch_16040(fcl)
 » show all
Taxonomy
Reference
1  [PMID:9465123]
  Authors
Essigmann B, Guler S, Narang RA, Linke D, Benning C.
  Title
Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana.
  Journal
Proc Natl Acad Sci U S A 95:1950-5 (1998)
DOI:10.1073/pnas.95.4.1950
  Sequence
[ath:AT4G33030]
Reference
2  [PMID:10462438]
  Authors
Essigmann B, Hespenheide BM, Kuhn LA, Benning C.
  Title
Prediction of the active-site structure and NAD(+) binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis.
  Journal
Arch Biochem Biophys 369:30-41 (1999)
DOI:10.1006/abbi.1999.1344
Reference
3  [PMID:10557279]
  Authors
Mulichak AM, Theisen MJ, Essigmann B, Benning C, Garavito RM.
  Title
Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose.
  Journal
Proc Natl Acad Sci U S A 96:13097-102 (1999)
DOI:10.1073/pnas.96.23.13097
  Sequence
[ath:AT4G33030]
Reference
4  [PMID:11073956]
  Authors
Sanda S, Leustek T, Theisen MJ, Garavito RM, Benning C.
  Title
Recombinant Arabidopsis SQD1 converts udp-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro.
  Journal
J Biol Chem 276:3941-6 (2001)
DOI:10.1074/jbc.M008200200
  Sequence
[ath:AT4G33030]
Other DBs
ExplorEnz - The Enzyme Database: 3.13.1.1
IUBMB Enzyme Nomenclature: 3.13.1.1
ExPASy - ENZYME nomenclature database: 3.13.1.1
BRENDA, the Enzyme Database: 3.13.1.1

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