ATP synthase subunit alpha, mitochondrial (ATP synthase F1 subunit alpha)
1_MLSVR 6_ VAAAV 11_ VRALP 16_ RRAGL 21_ VSRNA 26_ LGSSF 31_ IAARN 36_ FHASN 41_ THLQK 46_ TGTAE 51_ MSSIL 56_ EERIL 61_ GADTS 66_ VDLEE 71_ TGRVL 76_ SIGDG 81_ IARVH 86_ GLRNV 91_ QAEEM 96_ VEFSS 101_ GLKGM 106_ SLNLE 111_ PDNVG 116_ VVVFG 121_ NDKLI 126_ KEGDI 131_ VKRTG 136_ AIVDV 141_ PVGEE 146_ LLGRV 151_ VDALG 156_ NAIDG 161_ KGPIG 166_ SKTRR 171_ RVGLK 176_ APGII 181_ PRISV 186_ REPMQ 191_ TGIKA 196_ VDSLV 201_ PIGRG 206_ QRELI 211_ IGDRQ 216_ TGKTS 221_ IAIDT 226_ IINQK 231_ RFNDG 236_ SDEKK 241_ KLYCI 246_ YVAIG 251_ QKRST 256_ VAQLV 261_ KRLTD 266_ ADAMK 271_ YTIVV 276_ SATAS 281_ DAAPL 286_ QYLAP 291_ YSGCS 296_ MGEYF 301_ RDNGK 306_ HALII 311_ YDDLS 316_ KQAVA 321_ YRQMS 326_ LLLRR 331_ PPGRE 336_ AYPGD 341_ VFYLH 346_ SRLLE 351_ RAAKM 356_ NDAFG 361_ GGSLT 366_ ALPVI 371_ ETQAG 376_ DVSAY 381_ IPTNV 386_ ISITD 391_ GQIFL 396_ ETELF 401_ YKGIR 406_ PAINV 411_ GLSVS 416_ RVGSA 421_ AQTRA 426_ MKQVA 431_ GTMKL 436_ ELAQY 441_ REVAA 446_ FAQFG 451_ SDLDA 456_ ATQQL 461_ LSRGV 466_ RLTEL 471_ LKQGQ 476_ YSPMA 481_ IEEQV 486_ AVIYA 491_ GVRGY 496_ LDKLE 501_ PSKIT 506_ KFENA 511_ FLSHV 516_ VSQHQ 521_ ALLGT 526_ IRADG 531_ KISEQ 536_ SDAKL 541_ KEIVT 546_NFLAG
1: Subunit alpha, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed:37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159)