Sequence of AK1BF_HUMAN
EC Number:1.1.1.36
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
Other sequences found for EC No. 1.1.1.36
EC Number:1.1.1.54
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
allyl alcohol + NADP+ = acrolein + NADPH + H+
Other sequences found for EC No. 1.1.1.54
EC Number:1.1.1.62
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
17beta-estradiol + NAD(P)+ = estrone + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.62
EC Number:1.1.1.64
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
testosterone + NADP+ = androstenedione + NADPH + H+
Other sequences found for EC No. 1.1.1.64
EC Number:1.1.1.216
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(2E,6E)-farnesol + NADP+ = (2E,6E)-farnesal + NADPH + H+
Other sequences found for EC No. 1.1.1.216
EC Number:1.1.1.300
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
retinol + NADP+ = retinal + NADPH + H+
Other sequences found for EC No. 1.1.1.300
General information:
Sequence
0 MATFVELSTK AKMPIVGLGT WRSLLGKVKE AVKVAIDAEY RHIDCAYFYE NQHEVGEAIQ
60 EKIQEKAVMR EDLFIVSKVW PTFFERPLVR KAFEKTLKDL KLSYLDVYLI HWPQGFKTGD
120 DFFPKDDKGN MISGKGTFLD AWEAMEELVD EGLVKALGVS NFNHFQIERL LNKPGLKYKP
180 VTNQVECHPY LTQEKLIQYC HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK
240 HKKTTAQVLI RFHIQRNVTV IPKSMTPAHI VENIQVFDFK LSDEEMATIL SFNRNWRAFD
300 FKEFSHLEDF PFDAEY
Download this sequence
Download all sequences for 1.1.1.300
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
512864
Salabei J.K.,Li X.P.,Petrash J.M.,Bhatnagar A.,Barski O.A.
Functional expression of novel human and murine AKR1B genes.
Chem. Biol. Interact.
191
177-184
2011
512865
Hillier L.W.,Fulton R.S.,Fulton L.A.,Graves T.A.,Pepin K.H.,Wagner-McPherson C.,Layman D.,Maas J.,Jaeger S.,Walker R.,Wylie K.,Sekhon M.,Becker M.C.,O'Laughlin M.D.,Schaller M.E.,Fewell G.A.,Delehaunty K.D.,Miner T.L.,Nash W.E.,Cordes M.,Du H.,Sun H.,Edwards J.,Bradshaw-Cordum H.,Ali J.,Andrews S.,Isak A.,Vanbrunt A.,Nguyen C.,Du F.,Lamar B.,Courtney L.,Kalicki J.,Ozersky P.,Bielicki L.,Scott K.,Holmes A.,Harkins R.,Harris A.,Strong C.M.,Hou S.,Tomlinson C.,Dauphin-Kohlberg S.,Kozlowicz-Reilly A.,Leonard S.,Rohlfing T.,Rock S.M.,Tin-Wollam A.-M.,Abbott A.,Minx P.,Maupin R.,Strowmatt C.,Latreille P.,Miller N.,Johnson D.,Murray J.,Woessner J.P.,Wendl M.C.,Yang S.-P.,Schultz B.R.,Wallis J.W.,Spieth J.,Bieri T.A.,Nelson J.O.,Berkowicz N.,Wohldmann P.E.,Cook L.L.,Hickenbotham M.T.,Eldred J.,Williams D.,Bedell J.A.,Mardis E.R.,Clifton S.W.,Chissoe S.L.,Marra M.A.,Raymond C.,Haugen E.,Gillett W.,Zhou Y.,James R.,Phelps K.,Iadanoto S.,Bubb K.,Simms E.,Levy R.,Clendenning J.,Kaul R.,Kent W.J.,Furey T.S.,Baertsch R.A.,Brent M.R.,Keibler E.,Flicek P.,Bork P.,Suyama M.,Bailey J.A.,Portnoy M.E.,Torrents D.,Chinwalla A.T.,Gish W.R.,Eddy S.R.,McPherson J.D.,Olson M.V.,Eichler E.E.,Green E.D.,Waterston R.H.,Wilson R.K.
The DNA sequence of human chromosome 7.
Nature
424
157-164
2003
512867
Weber S.,Salabei J.K.,Moller G.,Kremmer E.,Bhatnagar A.,Adamski J.,Barski O.A.
Aldo-keto reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto reductase with activity towards steroids and 3-keto-acyl-coa conjugates.
J. Biol. Chem.
290
6531-6545
2015
512868
Gimenez-Dejoz J.,Kolar M.H.,Ruiz F.X.,Crespo I.,Cousido-Siah A.,Podjarny A.,Barski O.A.,Fanfrlik J.,Pares X.,Farres J.,Porte S.
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase.
PLoS ONE
10
0-0
2015