eF-site ID 1ado-A PDB Code 1ado Chain A click to enlarge Title FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE Classification LYASE Compound ALDOLASE Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY Description Functional site 1) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 2) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 3) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 4) chain A residue 42 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 5) chain A residue 146 type sequence K description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 6) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 7) chain A residue 187 type sequence E description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 8) chain A residue 229 type sequence K description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 9) chain A residue 270 type sequence L description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 10) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 11) chain A residue 272 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 12) chain A residue 273 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 13) chain A residue 300 type sequence S description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 14) chain A residue 301 type sequence Y description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 15) chain A residue 302 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 16) chain A residue 303 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 17) chain A residue 34 type catalytic sequence E description 222 source MCSA : MCSA1 18) chain A residue 147 type catalytic sequence W description 222 source MCSA : MCSA1 19) chain A residue 188 type catalytic sequence P description 222 source MCSA : MCSA1 20) chain A residue 190 type catalytic sequence I description 222 source MCSA : MCSA1 21) chain A residue 230 type catalytic sequence P description 222 source MCSA : MCSA1 22) chain A residue 301 type catalytic sequence Y description 222 source MCSA : MCSA1 23) chain A residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 230 type ACT_SITE sequence P description Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 28) chain A residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 29) chain A residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 32) chain A residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 33) chain A residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 34) chain A residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 35) chain A residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 36) chain A residue 361 type MOD_RES sequence H description Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 source Swiss-Prot : SWS_FT_FI15 37) chain A residue 42 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI16 38) chain A residue 221-231 type prosite sequence IYLEGTLLKPN description ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN source prosite : PS00158 39) chain A residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 40) chain A residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 41) chain A residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 42) chain A residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 43) chain A residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 44) chain A residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 45) chain A residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 46) chain A residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 47) chain A residue 362 type SITE sequence A description Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base source Swiss-Prot : SWS_FT_FI6

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