KEGG   ENZYME: 1.2.1.80
Entry
EC 1.2.1.80                 Enzyme                                 
Name
long-chain acyl-[acyl-carrier-protein] reductase;
long-chain acyl-[acp] reductase;
fatty acyl-[acyl-carrier-protein] reductase;
acyl-[acp] reductase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
Sysname
long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming)
Reaction(IUBMB)
a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+ [RN:R09484 R09485]
Reaction(KEGG)
R09484 R09485
Substrate
long-chain aldehyde [CPD:C00609];
[acyl-carrier protein] [CPD:C00229];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
long-chain acyl-[acyl-carrier protein] [CPD:C20683];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
History
EC 1.2.1.80 created 2011
Orthology
K14330  fatty aldehyde-generating acyl-ACP reductase
Genes
VFFVITFI_CDS1482
DALKDSCA_06500
BTSBtus_0602
TUMCBW65_22005
TABCIG75_07705
EFFskT53_34800
CACECACET_c35020
CFMBJL90_03040
AMTAmet_4316
AOEClos_2418
GFEGferi_18430
CALEFDN13_03935
DCADesca_0167
PTHPTH_0261
DRMDred_0173
DRUDesru_0253
DFGB0537_01670
DAEDtox_0249
DKUDesku_3197
DAUDaud_0129
TFRBR63_14590
FWADCMF_21965
DGIDesgi_0316
HMOHM1_0645
HCVFTV88_2683
ACAEHYG86_08625
SAYTPY_0442
SAPSulac_0405
STHRBXT84_04875
CTHMCFE_0104
TTETTE2374
TEXTeth514_0808
THXThet_2108
TPDTeth39_0316
TITThit_2042
TMTTmath_1999
TBOThebr_0326
TWIThewi_2315
TKITKV_c21150
CHYCHY_2367
ADGAdeg_1649
TPZTph_c26210
TTMTthe_0378
TTOThethe_00327
TXYThexy_0276
TSHTsac_0954
TEPTepRe1_2126
TAETepiRe1_2289
TOCToce_2079
NTHNther_0115
HORHore_00730
HALSD7D81_00030
IFNGM661_16005
AARAcear_0121
HHLHalha_0143
AFTBBF96_15620
KMEH0A61_01195(pigE_1)
PUFUFO1_0509
PFTJBW_03936
MANAMAMMFC1_01979
STEDSPTER_48640(hemA_2)
PFACPFJ30894_02364
CFICelf_0203
ORNDV701_10430
MGGMPLG2_3309
SYNsll0209
SYZMYO_122770
SYYSYNGTS_2251(sll0209)
SYTSYNGTI_2250(sll0209)
SYSSYNPCCN_2249(sll0209)
SYQSYNPCCP_2249(sll0209)
SYJD082_05320
SYOC7I86_11770
SYCsyc0051_d
SYUM744_09025
SYFSynpcc7942_1594
SYDSyncc9605_0729
SYESyncc9902_1634
SYGsync_1989
SYRSynRCC307_1585
SYXSynWH7803_0655
CYACYA_0414
CYBCYB_2441
SYNESyn6312_1511
SYNPSyn7502_03277
SYNKKR100_05370
SYNRKR49_12750
SYNDKR52_13295
SYHSyncc8109_1975
SYNWSynWH8103_01988(cACR)
SYNCCB0101_04555
SYNYBM449_13775
DSLDacsa_2180
SYWSYNW1737
CGCCyagr_0038
CYICBM981_0850
PMAPro_0533
PMMPMM0533
PMTPMT_1230
PMNPMN2A_1864
PMIPMT9312_0533
PMBA9601_05891
PMCP9515_05971
PMFP9303_07811
PMGP9301_05591
PMHP9215_06141
PMJP9211_05361
PMENATL1_05891
PRCEW14_0579
PRMEW15_0630
CMPCha6605_5417
AMRAM1_4042
WNAKA717_25575
TVNNIES2134_112430
SLWBRW62_00115
TELtll1312
THNNK55_03190
THECFFX45_09775
LENLEP3755_23580
LETO77CONTIG1_02794
LBOLBWT_14410
KOVK9N68_11175
LSCKIK02_13610
LSKJ5X98_02330
PSEUPse7367_3627
PSERABRG53_3066
THEUHPC62_16890
GLPGlo7428_0151
GEEGM3708_2119
MARMAE_53080
MPKVL20_1524
MIQB5D77_20955
MVZmyaer102_25850
CANCyan10605_1068
HAOPCC7418_0960
ENNFRE64_14815
CYUUCYN_05800
CYTcce_1430
CWACwatDRAFT_3385
CYPPCC8801_0872
CYHCyan8802_0898
CYNCyan7425_0399
TERTery_2279
ARPNIES39_M01920
PAGHNIES204_11580
PPSUNO713_00868
OXYHCG48_15930
MVAGD0A34_07470
LFSHFV01_13725
MICMic7113_4537
GEIGEI7407_1565
OACOscil6304_2073
ONIOsc7112_0945
PHORJWS08_08195
PYHNEA10_04670
CEPCri9333_4415
GVIgll3145
GLJGKIL_0726(hemA)
GMLISF26_16240
ANAalr5284
NPUNpun_R1710
NOSNos7107_1027
NOPNos7524_4305
NONNOS3756_54750
NFLCOO91_03201
NOECLI64_08840
NSHGXM_04006
NEDHUN01_28130
AVAAva_2534
NAZAazo_3370
ANBANA_C11209
ACYAnacy_3390
AWAAA650_00530
ANNEH233_18780
CSGCylst_0696
RSINB6N60_03103
CALOCal7507_5585
CALTCal6303_4370
CALHIJ00_07395
CALNNIES2098_27730
RIVRiv7116_3791
FISFIS3754_06320
NSPHBDGGKGIB_04212
DOUBMF77_02262
DFSHGD76_06325
DHTNG743_14495
CCURIAR63_11975
CRKL3I90_01360
AFLOHEQ12_03500
TOQHCG51_19275
NCNBZZ01_14985
CTHEChro_1553
CEOETSB_0189
CERRGRSB_0136
THUGKNN16_02140
DMRDeima_1953
DCHSY84_14815
DGADEGR_12050
CCZCCALI_02334
FGIOP10G_3716
NPYNPRO_00590
RHOZGXP67_04260
DFEDfer_5680
ADDHUW48_09010
CPOCOPRO5265_1114
NMVNITMOv2_1388
 » show all
Reference
1  [PMID:20671186]
  Authors
Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB
  Title
Microbial biosynthesis of alkanes.
  Journal
Science 329:559-62 (2010)
DOI:10.1126/science.1187936
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.80
IUBMB Enzyme Nomenclature: 1.2.1.80
ExPASy - ENZYME nomenclature database: 1.2.1.80
BRENDA, the Enzyme Database: 1.2.1.80

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