DHSO_CHICK
ID DHSO_CHICK Reviewed; 355 AA.
AC P0DMQ6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:15649778};
DE Short=SDH {ECO:0000303|PubMed:15649778};
DE EC=1.1.1.- {ECO:0000269|PubMed:15649778};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
GN Name=SORD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=15649778; DOI=10.1016/j.cbpc.2004.10.017;
RA Karacaoglan V., Ozer I.;
RT "Steady-state kinetic properties of sorbitol dehydrogenase from chicken
RT liver.";
RL Comp. Biochem. Physiol. 140:309-312(2005).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)-
CC dependent oxidation of various sugar alcohols. Is active with D-
CC sorbitol (D-glucitol) as substrate, leading to the C2-oxidized product
CC D-fructose (PubMed:15649778). Is a key enzyme in the polyol pathway
CC that interconverts glucose and fructose via sorbitol, which constitutes
CC an important alternate route for glucose metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q00796, ECO:0000269|PubMed:15649778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+);
CC Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:15649778};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07846};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P07846};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for NAD(+) (at 25 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15649778};
CC KM=3.2 mM for sorbitol (at 25 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15649778};
CC KM=240 uM for NADH (at 25 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15649778};
CC KM=1000 mM for D-fructose (at 25 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:15649778};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07846}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q64442}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64442}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q64442}. Note=Associated with mitochondria of
CC the midpiece and near the plasma membrane in the principal piece of the
CC flagellum. {ECO:0000250|UniProtKB:Q64442}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:15649778}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; JH374619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DMQ6; -.
DR SMR; P0DMQ6; -.
DR STRING; 9031.ENSGALP00000003637; -.
DR PaxDb; P0DMQ6; -.
DR Ensembl; ENSGALT00000058793; ENSGALP00000049830; ENSGALG00000031408.
DR VEuPathDB; HostDB:geneid_415332; -.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00550000074781; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR OMA; ETWYAMS; -.
DR OrthoDB; 1019156at2759; -.
DR Reactome; R-GGA-5652227; Fructose biosynthesis.
DR Reactome; R-GGA-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:P0DMQ6; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000031408; Expressed in kidney and 13 other tissues.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IDA:AgBase.
DR GO; GO:0051287; F:NAD binding; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046370; P:fructose biosynthetic process; NAS:AgBase.
DR GO; GO:0006000; P:fructose metabolic process; IDA:AgBase.
DR GO; GO:0006116; P:NADH oxidation; IDA:AgBase.
DR GO; GO:0006735; P:NADH regeneration; IDA:AgBase.
DR GO; GO:0006061; P:sorbitol biosynthetic process; NAS:AgBase.
DR GO; GO:0006062; P:sorbitol catabolic process; IDA:AgBase.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cilium; Flagellum; Membrane; Metal-binding;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT CHAIN 2..355
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000431067"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 295..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
SQ SEQUENCE 355 AA; 38144 MW; B8F91CFF6901319F CRC64;
MAATGQNLAV VVHRAGDLRL ENRPIPEPGP NEVLLRMHSV GICGSDVHYW QHGRIGDFVV
KDPMVLGHEA SGTVIKVGAG VTHLKPGDRV AIEPGVPRET DEFCKTGRYN LSPTIFFCAT
PPDDGNLCRY YKHSASYCYK LPDSVTFEEG ALIEPLSVGI HACKRAGVTL GSRVFVSGSG
PIGLVNVIIA KMMGAAAVVV TDLSASRLQT AKELGADFTI QIKNETPQEV AAKVESLLGC
MPEITVECTG VQACIQASIY ATRSGGTLVL VGLGPEMVTV PIVNAAVREV DIRGIFRYCN
TWPVAISLLA SKRINIKPLV THRFPLEKAL EAFETTKRGE GVKIMLKCDP TDQNP
