Serine palmitoyltransferase 3 (EC 2.3.1.50) (Long chain base biosynthesis protein 2b) (LCB2b) (Long chain base biosynthesis protein 3) (LCB 3) (Serine-palmitoyl-CoA transferase 3) (SPT 3)
1_MANPG 6_ GGAVC 11_ NGKLH 16_ NHKKQ 21_ SNGSQ 26_ SRNCT 31_ KNGIV 36_ KEAQQ 41_ NGKPH 46_ FYDKL 51_ IVESF 56_ EEAPL 61_ HVMVF 66_ TYMGY 71_ GIGTL 76_ FGYLR 81_ DFLRN 86_ WGIEK 91_ CNAAV 96_ ERKEQ 101_ KDFVP 106_ LYQDF 111_ ENFYT 116_ RNLYM 121_ RIRDN 126_ WNRPI 131_ CSAPG 136_ PLFDL 141_ MERVS 146_ DDYNW 151_ TFRFT 156_ GRVIK 161_ DVINM 166_ GSYNF 171_ LGLAA 176_ KYDES 181_ MRTIK 186_ DVLEV 191_ YGTGV 196_ ASTRH 201_ EMGTL 206_ DKHKE 211_ LEDLV 216_ AKFLN 221_ VEAAM 226_ VFGMG 231_ FATNS 236_ MNIPA 241_ LVGKG 246_ CLILS 251_ DELNH 256_ TSLVL 261_ GARLS 266_ GATIR 271_ IFKHN 276_ NTQSL 281_ EKLLR 286_ DAVIY 291_ GQPRT 296_ RRAWK 301_ KILIL 306_ VEGVY 311_ SMEGS 316_ IVHLP 321_ QIIAL 326_ KKKYK 331_ AYLYI 336_ DEAHS 341_ IGAVG 346_ PTGRG 351_ VTEFF 356_ GLDPH 361_ EVDVL 366_ MGTFT 371_ KSFGA 376_ SGGYI 381_ AGRKD 386_ LVDYL 391_ RVHSH 396_ SAVYA 401_ SSMSP 406_ PIAEQ 411_ IIRSL 416_ KLIMG 421_ LDGTT 426_ QGLQR 431_ VQQLA 436_ KNTRY 441_ FRQRL 446_ QEMGF 451_ IIYGN 456_ ENASV 461_ VPLLL 466_ YMPGK 471_ VAAFA 476_ RHMLE 481_ KKIGV 486_ VVVGF 491_ PATPL 496_ AEARA 501_ RFCVS 506_ AAHTR 511_ EMLDT 516_ VLEAL 521_ DEMGD 526_ LLQLK 531_ YSRHK 536_ KSARP 541_ ELYDE 546_TSFEL
1: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650). The SPT complex is composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference (PubMed:19416851). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference (PubMed:19416851, PubMed:19648650)