KEGG   ENZYME: 1.2.1.76
Entry
EC 1.2.1.76                 Enzyme                                 
Name
succinate-semialdehyde dehydrogenase (acylating);
succinyl-coA reductase;
coenzyme-A-dependent succinate-semialdehyde dehydrogenase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
Sysname
succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating)
Reaction(IUBMB)
succinate semialdehyde + CoA + NADP+ = succinyl-CoA + NADPH + H+ [RN:R09280]
Reaction(KEGG)
R09280
Substrate
succinate semialdehyde [CPD:C00232];
CoA [CPD:C00010];
NADP+ [CPD:C00006]
Product
succinyl-CoA [CPD:C00091];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde. The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation [1], and in Metallosphaera sedula, where it participates in the 3-hydroxypropanonate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
History
EC 1.2.1.76 created 2009
Pathway
ec00650  Butanoate metabolism
ec00720  Carbon fixation pathways in prokaryotes
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K15017  malonyl-CoA/succinyl-CoA reductase (NADPH)
K15038  succinyl-CoA reductase
K18119  succinate-semialdehyde dehydrogenase
Genes
BGJAWC36_10870
BIZHC231_15390
CABASBC2_75930(sucD_2)
METIDK427_23010
EGVEGCR1_14565
EAVEH197_01765
ERAFJ9537_15030
AUNAWM73_02295
CKLCKL_3015(sucD)
CKRCKR_2663
CSQCSCA_3620
CEUA7L45_11960
CRSFQB35_12335
CPRFK7H06_01435 K7H06_15520
PFAAMM59RIKEN_18180(sucD_1) MM59RIKEN_18920(sucD_2) MM59RIKEN_21990(sucD_3) MM59RIKEN_24180(sucD_4) MM59RIKEN_28330(sucD_5) MM59RIKEN_28340(sucD_6)
LACYA4V08_31365
CPROCPRO_14650(sucD_1) CPRO_16270(sucD_2)
CDFCD630_23420(sucD)
PDCCDIF630_02581(sucD)
CDCCD196_2185(sucD)
CDLCDR20291_2231(sucD)
PDFCD630DERM_23420(sucD)
CMIUB1H56_01435
HASHalsa_0175
ERLAOC36_06545
MBFBHV42_01465
PGIPG_0687(sucD)
PGNPGN_0723
PGTPGTDC60_1813(sucD)
PAHPoras_0443
PCRENCTC12858_01805(sucD)
PCAGNCTC12856_01246(sucD)
PENDLA319_00245
PSOECE91St14_12650(sucD)
TFOBFO_1488
OSPOdosp_2058
BUYD8S85_11140
BVIRI6J59_04655
STOSTK_00640 STK_21710(mcr_scr)
SOHD1869_11875(asd) D1869_14740
SSOSSO1629(gapN-1) SSO1842(gapN-2) SSO2178(asd-2)
SOLSsol_2908
SSOASULA_2921(asd)
SSOLSULB_2921(asd)
SSOFSULC_2918(asd)
SSHIJ5U23_00989 J5U23_02098
SCASSACC_11800 SACC_21720
SAISaci_1738 Saci_2147 Saci_2370
SACNSacN8_08450 SacN8_10450 SacN8_11535
SACRSacRon12I_08465 SacRon12I_10705 SacRon12I_11780
SACSSUSAZ_08265 SUSAZ_09800 SUSAZ_11160
SISLS215_0550 LS215_2961
SIAM1425_1049 M1425_2796
SIMM1627_1112 M1627_2848
SIDM164_1027 M164_2777
SIYYG5714_1027 YG5714_2976
SINYN1551_1850 YN1551_2101 YN1551_3167
SIILD85_0963 LD85_1154 LD85_3126
SIHSiH_0568 SiH_2755
SIRSiRe_0909 SiRe_2691
SICSiL_0776 SiL_2637
SULABFU36_00640 BFU36_10310
SULEGFS03_01510(asd) GFS03_05485
SULOGFS33_06710(asd) GFS33_10785
SULLEWF20_01070 EWF20_13035(asd)
MSEMsed_0709 Msed_1119 Msed_1774
MCNMcup_1427
MHKDFR87_03300(asd) DFR87_09790 DFR87_12125
MPRUDFR88_00930 DFR88_03035(asd) DFR88_09350
MTENGWK48_02495 GWK48_08305(asd)
MJNMjAS7_1475 MjAS7_2925
MEMJMJ1HA_0819 MJ1HA_1248 MJ1HA_2026
AHOAhos_0324 Ahos_2348
AMANB6F84_02355 B6F84_04975 B6F84_05470
ABRIDFR85_01565(asd) DFR85_12665 DFR85_14580
ASULDFR86_02340(asd)
AAMBD1866_06835(asd)
ACIHHS5_12500
SAZOD1868_09095(asd)
CSTYKN1_05910 KN1_13950
STEPIC006_0038
SAHSHS7_03090
PISPisl_0249
PCLPcal_1387
PYRP186_0719
POGPogu_1297
TNETneu_0421
PYWPYWP30_00439
CMACmaq_0073
TTNTTX_1101
TUZTUZN_0139 TUZN_0951
CCAINAS2_0171
 » show all
Reference
1  [PMID:8444151]
  Authors
Sohling B, Gottschalk G
  Title
Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri.
  Journal
Eur J Biochem 212:121-7 (1993)
DOI:10.1111/j.1432-1033.1993.tb17641.x
  Sequence
Reference
2  [PMID:17041055]
  Authors
Alber B, Olinger M, Rieder A, Kockelkorn D, Jobst B, Hugler M, Fuchs G
  Title
Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp.
  Journal
J Bacteriol 188:8551-9 (2006)
DOI:10.1128/JB.00987-06
Reference
3  [PMID:18079405]
  Authors
Berg IA, Kockelkorn D, Buckel W, Fuchs G
  Title
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.
  Journal
Science 318:1782-6 (2007)
DOI:10.1126/science.1149976
  Sequence
[mse:Msed_0709]
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.76
IUBMB Enzyme Nomenclature: 1.2.1.76
ExPASy - ENZYME nomenclature database: 1.2.1.76
BRENDA, the Enzyme Database: 1.2.1.76

DBGET integrated database retrieval system