PGDH_MOUSE
ID PGDH_MOUSE Reviewed; 269 AA.
AC Q8VCC1; Q61106;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)];
DE Short=15-PGDH;
DE EC=1.1.1.141 {ECO:0000305|PubMed:8950170};
DE AltName: Full=Eicosanoid/docosanoid dehydrogenase [NAD(+)];
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P15428};
DE EC=1.1.1.232 {ECO:0000250|UniProtKB:P15428};
DE AltName: Full=Prostaglandin dehydrogenase 1;
GN Name=Hpgd; Synonyms=Pgdh1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=8950170; DOI=10.1016/s0167-4781(96)00123-6;
RA Matsuo M., Ensor C.M., Tai H.H.;
RT "Cloning and expression of the cDNA for mouse NAD(+)-dependent 15-
RT hydroxyprostaglandin dehydrogenase.";
RL Biochim. Biophys. Acta 1309:21-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=20448048; DOI=10.1074/jbc.m109.084426;
RA Shiraya K., Hirata T., Hatano R., Nagamori S., Wiriyasermkul P.,
RA Jutabha P., Matsubara M., Muto S., Tanaka H., Asano S., Anzai N., Endou H.,
RA Yamada A., Sakurai H., Kanai Y.;
RT "A novel transporter of SLC22 family specifically transports prostaglandins
RT and co-localizes with 15-hydroxyprostaglandin dehydrogenase in renal
RT proximal tubules.";
RL J. Biol. Chem. 285:22141-22151(2010).
CC -!- FUNCTION: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a
CC broad array of hydroxylated polyunsaturated fatty acids (mainly
CC eicosanoids and docosanoids, including prostaglandins, lipoxins and
CC resolvins), yielding their corresponding keto (oxo) metabolites (By
CC similarity) (PubMed:8950170). Decreases the levels of the pro-
CC proliferative prostaglandins such as prostaglandin E2 (whose activity
CC is increased in cancer because of an increase in the expression of
CC cyclooxygenase 2) and generates oxo-fatty acid products that can
CC profoundly influence cell function by abrogating pro-inflammatory
CC cytokine expression. Converts resolvins E1, D1 and D2 to their oxo
CC products, which represents a mode of resolvin inactivation. Resolvin E1
CC plays important roles during the resolution phase of acute
CC inflammation, while resolvins D1 and D2 have a unique role in obesity-
CC induced adipose inflammation (By similarity).
CC {ECO:0000250|UniProtKB:P15428, ECO:0000269|PubMed:8950170}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) +
CC NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564;
CC EC=1.1.1.141; Evidence={ECO:0000305|PubMed:8950170};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877;
CC Evidence={ECO:0000305|PubMed:8950170};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + NAD(+) = 15-
CC oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:23260, ChEBI:CHEBI:15378, ChEBI:CHEBI:57409,
CC ChEBI:CHEBI:57410, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.232; Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + NAD(+) = 11-
CC oxo-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:48640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78836, ChEBI:CHEBI:90697;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lipoxin A4 + NAD(+) = 15-oxo-(5S,6R)-dihydroxy-
CC (7E,9E,11Z,13E)-eicosatetraenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:41572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:67026, ChEBI:CHEBI:78311;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate + H(+) +
CC NADH = (5S,6R,15S)-trihydroxy-(7E,9E,11Z)-eicosatrienoate + NAD(+);
CC Xref=Rhea:RHEA:41596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78325, ChEBI:CHEBI:78329;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prostaglandin A1 = 15-oxo-prostaglandin A1 + H(+) +
CC NADH; Xref=Rhea:RHEA:41263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57398,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85072;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) +
CC NADH; Xref=Rhea:RHEA:16477, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC ChEBI:CHEBI:57401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=14-hydroxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + NAD(+) =
CC 14-oxo-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:48952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:90866, ChEBI:CHEBI:90867;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + resolvin E1 = 18-oxo-resolvin E1 + H(+) + NADH;
CC Xref=Rhea:RHEA:49244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:91000, ChEBI:CHEBI:91001;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + resolvin D1 = 8-oxoresolvin D1 + H(+) + NADH;
CC Xref=Rhea:RHEA:50124, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132080;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + resolvin D1 = 17-oxoresolvin D1 + H(+) + NADH;
CC Xref=Rhea:RHEA:50128, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132081;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + resolvin D2 = 7-oxoresolvin D2 + H(+) + NADH;
CC Xref=Rhea:RHEA:53584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137497;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + resolvin D2 = 16-oxoresolvin D2 + H(+) + NADH;
CC Xref=Rhea:RHEA:53588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137498;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589;
CC Evidence={ECO:0000250|UniProtKB:P15428};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in proximal convoluted tubules of the
CC kidney, where it colocalizes with the prostaglandin transporter
CC SLC22A22 (at protein level) (PubMed:20448048). Expressed in lung,
CC intestine, stomach and liver (PubMed:8950170).
CC {ECO:0000269|PubMed:20448048, ECO:0000269|PubMed:8950170}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41825.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44389; AAB41825.1; ALT_FRAME; mRNA.
DR EMBL; AK146038; BAE26850.1; -; mRNA.
DR EMBL; BC021157; AAH21157.1; -; mRNA.
DR CCDS; CCDS40341.1; -.
DR RefSeq; NP_032304.2; NM_008278.2.
DR AlphaFoldDB; Q8VCC1; -.
DR SMR; Q8VCC1; -.
DR STRING; 10090.ENSMUSP00000034026; -.
DR BindingDB; Q8VCC1; -.
DR iPTMnet; Q8VCC1; -.
DR PhosphoSitePlus; Q8VCC1; -.
DR jPOST; Q8VCC1; -.
DR MaxQB; Q8VCC1; -.
DR PaxDb; Q8VCC1; -.
DR PeptideAtlas; Q8VCC1; -.
DR PRIDE; Q8VCC1; -.
DR ProteomicsDB; 288131; -.
DR Antibodypedia; 1511; 585 antibodies from 38 providers.
DR DNASU; 15446; -.
DR Ensembl; ENSMUST00000034026; ENSMUSP00000034026; ENSMUSG00000031613.
DR GeneID; 15446; -.
DR KEGG; mmu:15446; -.
DR UCSC; uc009lso.1; mouse.
DR CTD; 3248; -.
DR MGI; MGI:108085; Hpgd.
DR VEuPathDB; HostDB:ENSMUSG00000031613; -.
DR eggNOG; KOG4169; Eukaryota.
DR GeneTree; ENSGT00940000154593; -.
DR HOGENOM; CLU_010194_2_16_1; -.
DR InParanoid; Q8VCC1; -.
DR OMA; QGIHFQN; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; Q8VCC1; -.
DR TreeFam; TF324093; -.
DR Reactome; R-MMU-2142700; Synthesis of Lipoxins (LX).
DR Reactome; R-MMU-9018676; Biosynthesis of D-series resolvins.
DR Reactome; R-MMU-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR BioGRID-ORCS; 15446; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hpgd; mouse.
DR PRO; PR:Q8VCC1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VCC1; protein.
DR Bgee; ENSMUSG00000031613; Expressed in right lung lobe and 203 other tissues.
DR Genevisible; Q8VCC1; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISO:MGI.
DR GO; GO:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB.
DR GO; GO:0097070; P:ductus arteriosus closure; IMP:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0030728; P:ovulation; ISS:UniProtKB.
DR GO; GO:0007567; P:parturition; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:1905828; P:regulation of prostaglandin catabolic process; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid metabolism; Lipid metabolism; NAD; Oxidoreductase;
KW Prostaglandin metabolism; Reference proteome; Tumor suppressor.
FT CHAIN 1..269
FT /note="15-hydroxyprostaglandin dehydrogenase [NAD(+)]"
FT /id="PRO_0000253626"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 12..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 36..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 63..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="S -> G (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> S (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="E -> G (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="T -> A (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="N -> D (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="A -> P (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="T -> S (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> E (in Ref. 1; AAB41825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 29181 MW; 10E879A7E31A8E34 CRC64;
MHVNGKVALV TGAAQGIGKA FAEALLLHGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF
VQCDVADQKQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EQTLQINLVS VISGTYLGLD
YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIIG FTRSAAMAAN LMKSGVRLNV
ICPGFVDTPI LESIEKEENM GQYIEYKDQI KAMMKFYGVL HPSTIANGLI NLIEDDALNG
AIMKITASKG IHFQDYDISP LLVKAPLTS
