KEGG   ENZYME: 1.1.1.313
Entry
EC 1.1.1.313                Enzyme                                 
Name
sulfoacetaldehyde reductase (NADPH);
isfD (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
isethionate:NADP+ oxidoreductase
Reaction(IUBMB)
isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+ [RN:R02600]
Reaction(KEGG)
R02600
Substrate
isethionate [CPD:C05123];
NADP+ [CPD:C00006]
Product
2-sulfoacetaldehyde [CPD:C00593];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433, sulfoacetaldehyde reductase (NADH).
History
EC 1.1.1.313 created 2011, modified 2022
Pathway
ec00430  Taurine and hypotaurine metabolism
ec01100  Metabolic pathways
Orthology
K15373  sulfoacetaldehyde reductase
Genes
ENRH650_21530
ENFAKI40_3718
KPNKPN_00576
KPUKP1_1516
KPMKPHS_14060
KPPA79E_3668
KPHKPNIH24_21755
KPZKPNIH27_06510
KPVKPNIH29_07210
KPWKPNIH30_07240
KPYKPNIH31_07125
KPGKPNIH32_07345
KPCKPNIH10_07035
KPQKPR0928_06945
KPTVK055_1961(sdh)
KPOKPN2242_05720
KPRKPR_3984
KPJN559_3751
KPID364_02995
KPAKPNJ1_04010
KPXPMK1_02903(isfD)
KPBFH42_23905
KPNEKU54_019415
KPNULI86_19240
KPNKBN49_1630
KVAKvar_3797
KPEKPK_4008
KPKA593_17310
KVDKR75_14770
KVQSP68_21400
KOXKOX_13770
KOEA225_1573
KOYJ415_23770
KOMHR38_12515
KOKKONIH1_07720
KOCAB185_28375
KQUAVR78_11510
KLLBJF97_08105
KLWDA718_20615
KARLGL98_18440
KGRJJJ10_20430
KPASLUW96_14500
KLCK7H21_20455
KLMBWI76_07595
REEelectrica_03726(isfD)
RORRORB6_12190
RONTE10_08740
RPLNB1209_19890
RAODSD31_18740
RTGNCTC13098_05468(sdh)
PGELG71_22100
KSAC813_08935
KORAWR26_18435
KRDA3780_05845
KPSEIP581_05955
KOOO9K67_18310
KOUC0557_06255
KGOCEW81_17995
KIENCTC12125_02387(sdh)
KASKATP_32820
KLUK7B04_11875
KCYRIN60_16890
KINAB182_18395
PDZHHA33_20875
METYMRY16398_41760
PVJLMA04_06695
SUPEP0H77_06935
EBCC2U52_29615
EBUCUC76_08560
SERASer39006_001610
SERQCWC46_01610
DAQDAQ1742_04400
DLCO1Q98_12030
DDADd703_0033
BGJAWC36_18995
BRBEH207_00165
BNGEH206_00325
PRODPCO85_00670
LBQCKQ53_05475
LPOPI6N93_00125
VNAPN96_16100
VEJVEJY3_24206
VBRA6E01_10135
VCCFAZ90_18230
VASGT360_16430
VZIG5S32_21200
VOSKNV97_10020
VCRAIS519_17345
PGBH744_1c1567
PPSEBN5_0584
PFVPsefu_4080
PRHLT40_19355
PSESPSCI_0298
PALLUYA_03345
PSEJHNQ25_20830
PKHJLK41_03575
PTYJWV26_14350
PPHNHU825_04595
PCHEQYM18_11210
PSAPST_4121
PSZPSTAB_4103
PSRPSTAA_4273
PSCA458_00540
PSJPSJM300_18885
PSHPsest_0101
PSTTCH92_10795
PSTUUIB01_00490
PSEDDM292_19735
PCHLLLJ08_00490
PBMCL52_20375
PKGLW136_00495
SDEGGOM96_10015
PZDKQ248_07990
AVNAvin_16870 Avin_30890
AVLAvCA_16870 AvCA_30890
AVDAvCA6_16870 AvCA6_30890
ACXAchr_17360 Achr_26200
EMODM558_08540
EAZJHT90_10540
ENTOMTZ49_15490
HPEGEAO82_01580
HAESLO767_00655
HARRHV822_10695
PBAUOS670_13085
MSRAU15_02960
TZOTHMIRHAT_10700
SSALSPISAL_03475
CSACsal_0161 Csal_2684
CCAGSR908_04100 SR908_07265
HCSFF32_03330
HAKKO116_00630
HAMHALO0642
HSIBOX17_12380
HALOBWR19_05090 BWR19_11015
HHHCLM76_08275
HPROLMS44_20250
HQDK1Y77_15710
HALFQEN58_17610
HHAOQWG60_09720
HASOB2G49_15610
HASHHXW73_16000
HAMSNF683_03725
HALKCUU95_08810
HVNEI420_17320
HOLHORIV_63670
HSRHSBAA_60050
HPIZGYM47_15200
HNPSR894_18565
HTTHZS52_07980
HTXEKK97_11325
ZPLZBT109_2532
HAAA5892_16765
KUSB9G99_08575
KMAB9H00_06270
KUYFY550_02415 FY550_11870
SAJSQO259_04000
CDIZCEDIAZO_03401(isfD)
BOJCBF45_06055
ODIODI_R0192
KGYEHF36_06485
HGRDW355_05040
MMYRMXMO3_02929
AUAM673_19980
EBLAJGUZn3_01220(isfD)
 » show all
Reference
1  [PMID:20133363]
  Authors
Krejcik Z, Hollemeyer K, Smits TH, Cook AM
  Title
Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase.
  Journal
Microbiology 156:1547-55 (2010)
DOI:10.1099/mic.0.036699-0
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.313
IUBMB Enzyme Nomenclature: 1.1.1.313
ExPASy - ENZYME nomenclature database: 1.1.1.313
BRENDA, the Enzyme Database: 1.1.1.313

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