ID H0Z2V1_TAEGU Unreviewed; 355 AA.
AC H0Z2V1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000256|ARBA:ARBA00026132};
DE AltName: Full=Polyol dehydrogenase {ECO:0000256|ARBA:ARBA00032485};
GN Name=SORD {ECO:0000313|Ensembl:ENSTGUP00000004893.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000004893.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000004893.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000004893.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000256|ARBA:ARBA00004230}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004318}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004318}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR RefSeq; XP_002193475.1; XM_002193439.2.
DR AlphaFoldDB; H0Z2V1; -.
DR STRING; 59729.ENSTGUP00000004893; -.
DR Ensembl; ENSTGUT00000004942.2; ENSTGUP00000004893.2; ENSTGUG00000004734.2.
DR GeneTree; ENSGT00550000074781; -.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; H0Z2V1; -.
DR OMA; VCEMSGH; -.
DR OrthoDB; 3017546at2759; -.
DR TreeFam; TF313060; -.
DR Proteomes; UP000007754; Chromosome 10.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0047833; F:D-sorbitol dehydrogenase (acceptor) activity; IEA:Ensembl.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0046370; P:fructose biosynthetic process; IEA:Ensembl.
DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IEA:Ensembl.
DR GO; GO:0051160; P:L-xylitol catabolic process; IEA:Ensembl.
DR GO; GO:0006062; P:sorbitol catabolic process; IEA:Ensembl.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..346
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 355 AA; 38059 MW; 4CFA4004C7ABDAA5 CRC64;
MAAPGQNVAV VVHRAGELRL ENRPIPEPGP NEVLLRMHSV GICGSDVHYW QHGRIGDFVV
KDPMVLGHEA SGTVIKVGSG VTHLQPGDRV AIEPGVPREM DEFCKSGRYN LSPTIFFCAT
PPDDGNLCRY YKHSASYCYK LPDNVTFEEG ALIEPLSVGI HACKRAGVTL GSKVFVSGSG
PIGLVNVIVA KMMGAAVVVV TDLSASRLQK AKEVGADFTI QVKNETAQEV ASKVESVLGC
MPEITVECTG VQACIQAGIY ATRSGGTLVL VGLGPEMVTV PIVNAAVREV DIRGIFRYCN
TWPVAIALLA SKRINVKPLV THRFPLEKAL EAFETTKRGE GVKVMLKCDP TDQSP
//
