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ENZYME

ENZYME entry: EC 7.5.2.6

PURL: https://purl.expasy.org/enzyme/EC/7.5.2.6
Accepted Name
ABC-type lipid A-core oligosaccharide transporter
Alternative Name(s)
ATP-dependent lipid A-core flippase
lipid flippase
Reaction catalysed
ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2
Comment(s)
  • An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.
  • The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway.
  • Not to be confused with EC 7.5.2.5, which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process.
Cross-references
Rhea expert-curated reactions7.5.2.6
ExplorEnz7.5.2.6
IUBMB Enzyme Nomenclature7.5.2.6
UniProtKB/Swiss-Prot
Q483B6, MSBA1_COLP3Q480N3, MSBA2_COLP3Q6F9X0, MSBA_ACIAD
Q21WN9, MSBA_ALBFTQ0VQP5, MSBA_ALCBSQ5E0F2, MSBA_ALIF1
Q0A4U4, MSBA_ALKEHQ5P2S7, MSBA_AROAEQ7VR44, MSBA_BLOFL
Q492S9, MSBA_BLOPBQ2KYS6, MSBA_BORA1Q7WH20, MSBA_BORBR
Q7W9N7, MSBA_BORPAQ7VWD8, MSBA_BORPEQ39E73, MSBA_BURL3
Q62IG3, MSBA_BURMAQ1BUV6, MSBA_BURO1Q3JUI6, MSBA_BURP1
Q63VX7, MSBA_BURPSQ2SZW0, MSBA_BURTAQ1QX69, MSBA_CHRI1
Q7NZU6, MSBA_CHRVOQ83D84, MSBA_COXBUQ1LQD3, MSBA_CUPMC
Q46Y89, MSBA_CUPPJQ47JR8, MSBA_DECARQ6AJW3, MSBA_DESPS
P60753, MSBA_ECO57Q0TJD9, MSBA_ECOL5Q8FJB1, MSBA_ECOL6
P60752, MSBA_ECOLIQ1RDU4, MSBA_ECOUTQ47908, MSBA_FRANO
Q14JW6, MSBA_FRAT1Q2A1U9, MSBA_FRATHQ0BKJ3, MSBA_FRATO
Q5NIG3, MSBA_FRATTQ7VL52, MSBA_HAEDUQ4QPI4, MSBA_HAEI8
P44407, MSBA_HAEINQ2SIN5, MSBA_HAHCHQ0I4C5, MSBA_HISS1
Q31FG2, MSBA_HYDCUQ5QU36, MSBA_IDILOQ5X498, MSBA_LEGPA
Q5ZUH9, MSBA_LEGPHQ5WVN2, MSBA_LEGPLQ65U21, MSBA_MANSM
Q60AA3, MSBA_METCAQ1GZI0, MSBA_METFKQ5F4X8, MSBA_NEIG1
Q9JW59, MSBA_NEIMAQ9JXR3, MSBA_NEIMBQ3J7R8, MSBA_NITOC
Q142P6, MSBA_PARXLQ9CMG7, MSBA_PASMUQ6D437, MSBA_PECAS
Q7N6C6, MSBA_PHOLLQ6LPK6, MSBA_PHOPRQ12C33, MSBA_POLSJ
Q48P40, MSBA_PSE14Q15UY7, MSBA_PSEA6Q9HUG8, MSBA_PSEAE
Q4KJB2, MSBA_PSEF5Q3KJ31, MSBA_PSEPFQ88D92, MSBA_PSEPK
Q87VF3, MSBA_PSESMQ3IGX5, MSBA_PSET1Q4ZZ16, MSBA_PSEU2
Q4FS42, MSBA_PSYA2Q1QBW0, MSBA_PSYCKQ8XXB6, MSBA_RALN1
Q21NS8, MSBA_SACD2Q57R14, MSBA_SALCHQ5PGH0, MSBA_SALPA
P63360, MSBA_SALTIP63359, MSBA_SALTYQ12M46, MSBA_SHEDO
Q080T2, MSBA_SHEFNQ8EDF0, MSBA_SHEONQ0HHH4, MSBA_SHESM
Q0HTS8, MSBA_SHESRQ31YT6, MSBA_SHIBSQ32E34, MSBA_SHIDS
Q83LP0, MSBA_SHIFLQ3Z3K7, MSBA_SHISSQ2NUA5, MSBA_SODGM
Q2LVL0, MSBA_SYNASQ3SFZ6, MSBA_THIDAQ9KQW9, MSBA_VIBCH
Q87R16, MSBA_VIBPAQ8DAV2, MSBA_VIBVUQ7MJ07, MSBA_VIBVY
Q8D2U8, MSBA_WIGBRQ8PKS5, MSBA_XANACQ4UV65, MSBA_XANC8
Q8P8W4, MSBA_XANCPQ3BTC8, MSBA_XANE5Q2P3E7, MSBA_XANOM
Q5H0H0, MSBA_XANORQ9PEE7, MSBA_XYLFAQ87EF0, MSBA_XYLFT
Q1CA68, MSBA_YERPAQ8ZGA9, MSBA_YERPEQ1CGH0, MSBA_YERPN
Q66CI3, MSBA_YERPS
BRENDA7.5.2.6
MetaCyc7.5.2.6
KEGG Ligand Database for Enzyme Nomenclature7.5.2.6
EC2PDB7.5.2.6
MEDLINEFind literature relating to 7.5.2.6

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.5.2.-
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