Entry
Name
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase;
FA2H (gene name);
SCS7 (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With another compound as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
(4R)-4-hydroxysphinganine ceramide,ferrocytochrome-b5:oxygen oxidoreductase (fatty acyl 2-hydroxylating)
Reaction(IUBMB)
a phytoceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2'R)-2'-hydroxyphytoceramide + 2 ferricytochrome b5 + H2O [RN:
R11001 ]
Reaction(KEGG)
Substrate
Product
(2'R)-2'-hydroxyphytoceramide [CPD:
C21020 ];
ferricytochrome b5 [CPD:
C00996 ];
H2O [CPD:
C00001 ]
Comment
The enzyme, characterized from yeast and mammals, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis. The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The newly introduced 2-hydroxyl group has R-configuration. cf. EC
1.14.18.7 , dihydroceramide fatty acyl 2-hydroxylase.
History
EC 1.14.18.6 created 2015
Orthology
K19703 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase
Genes
PLEU : 114708073 114709106
SHAB : 115601096(FA2H) 115619010
XLA : 108715475(fa2h.S) 398669(fa2h.L)
SRX : 107707407 107707436 107714073
SANH : 107654164 107674969
CCAR : 109051125 109051187
CAUA : 113043051 113066797
CGIB : 127947104 128014301
MASI : 127436012 127437801
PFOR : 103142502 103142526
PLAI : 106937201 106940916
PMEI : 106907385 106931296
SSCO : 133981689 133982221
SASA : 106560925(fa2h) 106573787
STRU : 115151856 115196911
OGO : 123992064 124038012(fa2h)
OKI : 109867610(fa2h) 109888560
OMM : 135509475(fa2h) 135524509
OCLA : 139370722 139387024
SALP : 111952150 111962278
CCLU : 121531783 121577290
AANG : 118215231 118227032
AROT : 135241590 135255132
PSPA : 121296230 121325699
ARUT : 117424598 117425957
PSEX : 120515878 120542090(fa2h)
LCM : 102353320 102362617 102366970 102367411
PMRN : 116945979 116956093
DSI : Dsimw501_GD10257(Dsim_GD10257)
AALB : 109399104 109409914
TMOL : 138123042 138124420
CEL : CELE_C25A1.5(fath-1)
BMY : BM_BM2356(Bma-fath-1)
VPO : Kpol_1069p4 Kpol_541p9
NCS : NCAS_0C00470(NCAS0C00470)
NDI : NDAI_0K00470(NDAI0K00470)
TPF : TPHA_0C04710(TPHA0C04710)
TBL : TBLA_0D03180(TBLA0D03180)
TDL : TDEL_0B00680(TDEL0B00680)
KAF : KAFR_0B03850(KAFR0B03850)
KNG : KNAG_0J00320(KNAG0J00320)
DHA : DEHA2F00770g DEHA2F07304g
LBG : 92210471(LODBEIA_P52750)
CAL : CAALFM_C404590WA(SCS7)
ASAU : 88175734(PUMCH_004674)
YLI : 2908200(YALI2_F00728g)
NTE : NEUTE1DRAFT66051(NEUTE1DRAFT_66051)
SMP : 10801998(SMAC4_07221)
RTHE : 98127632(VTJ83DRAFT_6293)
FVR : FVEG_04833 FVEG_09980
TATV : 25775053(TrAtP1_000474)
TASP : 36614684(TrAFT101_001896)
PLJ : 28889025(PLICBS_008501)
PTKZ : JDV02_003079(SCS7_1) JDV02_006134(SCS7_2)
CDET : 87943074(CDEST_06571)
BFU : BCIN_03g04110(Bcscs7)
PTRR : 6348662(PtrM4_076980)
ADAC : 96081761(ACET3X_001439)
CDEC : 89991567(IAS62_004796)
CTEG : 91991924(I308_105068)
CBAS : 91985525(I312_105480)
CDEP : 91088658(L203_104448)
KMG : 30164345(I203_106054)
KNE : 92183545(IAR55_006287)
KDJ : 28964390(I303_100687)
KBI : 30206917(I302_103813)
KPIN : 30168974(I206_100722)
KSH : 87952876(IL334_000745)
KER : 91105871(V865_007070)
CCAC : CcaHIS019_0209410(SCS7)
SHS : STEHIDRAFT_119475 STEHIDRAFT_81527
HIR : HETIRDRAFT_481508(fa2h1)
ABP : AGABI1DRAFT116231(AGABI1DRAFT_116231)
ABV : AGABI2DRAFT194616(AGABI2DRAFT_194616)
SCM : SCHCO_02692030(SCHCODRAFT_02692030)
TET : TTHERM_00463850 TTHERM_00594230
LMAT : 92517923(LSCM1_08069)
LOI : 92364030(LSCM4_08226)
LEIS : 94183419(GH5_08208)
LEIN : 94191789(JIQ42_08228)
NPP : PP1Y_Lpl541 PP1Y_Mpl11096
» show all
Taxonomy
Reference
Authors
Mitchell AG, Martin CE
Title
Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids.
Journal
Sequence
Reference
Authors
Dunn TM, Haak D, Monaghan E, Beeler TJ
Title
Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain.
Journal
Sequence
Reference
Authors
Alderson NL, Rembiesa BM, Walla MD, Bielawska A, Bielawski J, Hama H
Title
The human FA2H gene encodes a fatty acid 2-hydroxylase.
Journal
Sequence
Reference
Authors
Eckhardt M, Yaghootfam A, Fewou SN, Zoller I, Gieselmann V
Title
A mammalian fatty acid hydroxylase responsible for the formation of alpha-hydroxylated galactosylceramide in myelin.
Journal
Sequence
Reference
Authors
Guo L, Zhang X, Zhou D, Okunade AL, Su X
Title
Stereospecificity of fatty acid 2-hydroxylase and differential functions of 2-hydroxy fatty acid enantiomers.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 1.14.18.6
LinkDB
All DBs