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Carotenoid isomerooxygenase (EC 1.13.11.65) (Beta-carotene 15,15'-monooxygenase and retinoid isomerase) (Beta-carotene dioxygenase and retinoid isomerase) (Neither inactivation nor afterpotential mutant B)

 NINAB_DROME             Reviewed;         620 AA.
Q9VFS2;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 127.
RecName: Full=Carotenoid isomerooxygenase;
EC=1.13.11.65;
AltName: Full=Beta-carotene 15,15'-monooxygenase and retinoid isomerase;
AltName: Full=Beta-carotene dioxygenase and retinoid isomerase;
AltName: Full=Neither inactivation nor afterpotential mutant B;
Name=ninaB; Synonyms=beta-diox; ORFNames=CG9347;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=10766819; DOI=10.1074/jbc.275.16.11915;
von Lintig J., Vogt K.;
"Filling the gap in vitamin A research. Molecular identification of an
enzyme cleaving beta-carotene to retinal.";
J. Biol. Chem. 275:11915-11920(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo, and Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION, AND MUTAGENESIS OF GLU-280; MET-471 AND GLU-477.
PubMed=11158606; DOI=10.1073/pnas.98.3.1130;
von Lintig J., Dreher A., Kiefer C., Wernet M.F., Vogt K.;
"Analysis of the blind Drosophila mutant ninaB identifies the gene
encoding the key enzyme for vitamin A formation invivo.";
Proc. Natl. Acad. Sci. U.S.A. 98:1130-1135(2001).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14982930; DOI=10.1074/jbc.M400323200;
Gu G., Yang J., Mitchell K.A., O'Tousa J.E.;
"Drosophila ninaB and ninaD act outside of retina to produce rhodopsin
chromophore.";
J. Biol. Chem. 279:18608-18613(2004).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17452532; DOI=10.1083/jcb.200610081;
Wang T., Jiao Y., Montell C.;
"Dissection of the pathway required for generation of vitamin A and
for Drosophila phototransduction.";
J. Cell Biol. 177:305-316(2007).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17344064; DOI=10.1016/j.mcn.2007.02.001;
Yang J., O'Tousa J.E.;
"Cellular sites of Drosophila NinaB and NinaD activity in vitamin A
metabolism.";
Mol. Cell. Neurosci. 35:49-56(2007).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=19889630; DOI=10.1074/jbc.M109.056101;
Voolstra O., Oberhauser V., Sumser E., Meyer N.E., Maguire M.E.,
Huber A., von Lintig J.;
"NinaB is essential for Drosophila vision but induces retinal
degeneration in opsin-deficient photoreceptors.";
J. Biol. Chem. 285:2130-2139(2010).
-!- FUNCTION: Catalyzes the oxidative cleavage at the 15,15'-double
bond of carotenoids and the simultaneous all-trans to 11-cis
isomerization of one cleavage product. Carotenoids like 11-cis
retinal can promote visual pigment biogenesis in the dark.
Essential for the biosynthesis of the 3-hydroxyretinal chromophore
of rhodopsin from zeaxanthin and for proper photoreceptor
development. Also essential for larval light perception.
{ECO:0000269|PubMed:11158606, ECO:0000269|PubMed:14982930,
ECO:0000269|PubMed:17344064, ECO:0000269|PubMed:17452532,
ECO:0000269|PubMed:19889630}.
-!- CATALYTIC ACTIVITY:
Reaction=all-trans-zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal
+ (3R)-all-trans-3-hydroxyretinal; Xref=Rhea:RHEA:33931,
ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:52228,
ChEBI:CHEBI:66898; EC=1.13.11.65;
Evidence={ECO:0000269|PubMed:10766819,
ECO:0000269|PubMed:19889630};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- PATHWAY: Cofactor metabolism; retinol metabolism.
-!- TISSUE SPECIFICITY: Expression follows organogenesis of the larval
Bolwig's organ (BO), which mediates larval photophobic behavior.
In the adult, expression is restricted exclusively to the brain.
Expressed in both neuronal cells and glia cells. Not active within
photoreceptors. Active within neuronal cells within the central
nervous system. {ECO:0000269|PubMed:10766819,
ECO:0000269|PubMed:14982930, ECO:0000269|PubMed:17344064,
ECO:0000269|PubMed:17452532, ECO:0000269|PubMed:19889630}.
-!- SIMILARITY: Belongs to the carotenoid oxygenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ276682; CAB93141.1; -; mRNA.
EMBL; AE014297; AAF54978.1; -; Genomic_DNA.
EMBL; AY121617; AAM51944.1; -; mRNA.
RefSeq; NP_650307.2; NM_142050.3.
UniGene; Dm.10048; -.
ProteinModelPortal; Q9VFS2; -.
IntAct; Q9VFS2; 1.
STRING; 7227.FBpp0082288; -.
PaxDb; Q9VFS2; -.
PRIDE; Q9VFS2; -.
EnsemblMetazoa; FBtr0082820; FBpp0082288; FBgn0002937.
GeneID; 41678; -.
KEGG; dme:Dmel_CG9347; -.
UCSC; CG9347-RA; d. melanogaster.
CTD; 41678; -.
FlyBase; FBgn0002937; ninaB.
eggNOG; KOG1285; Eukaryota.
eggNOG; COG3670; LUCA.
GeneTree; ENSGT00940000153415; -.
InParanoid; Q9VFS2; -.
KO; K18048; -.
OMA; QTNPNYA; -.
OrthoDB; EOG091G05GM; -.
PhylomeDB; Q9VFS2; -.
BioCyc; MetaCyc:MONOMER-17370; -.
BRENDA; 1.13.11.65; 1994.
BRENDA; 1.14.99.36; 1994.
Reactome; R-DME-2453902; The canonical retinoid cycle in rods (twilight vision).
Reactome; R-DME-975634; Retinoid metabolism and transport.
UniPathway; UPA00912; -.
GenomeRNAi; 41678; -.
PRO; PR:Q9VFS2; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0002937; Expressed in 11 organ(s), highest expression level in head.
ExpressionAtlas; Q9VFS2; baseline and differential.
Genevisible; Q9VFS2; DM.
GO; GO:0003834; F:beta-carotene 15,15'-monooxygenase activity; IDA:FlyBase.
GO; GO:0010436; F:carotenoid dioxygenase activity; IDA:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0004744; F:retinal isomerase activity; IDA:FlyBase.
GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
GO; GO:0016119; P:carotene metabolic process; IDA:FlyBase.
GO; GO:0055114; P:oxidation-reduction process; IDA:FlyBase.
GO; GO:0007602; P:phototransduction; TAS:FlyBase.
GO; GO:0007604; P:phototransduction, UV; IMP:FlyBase.
GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
GO; GO:0042574; P:retinal metabolic process; IDA:FlyBase.
GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0016063; P:rhodopsin biosynthetic process; IDA:FlyBase.
GO; GO:0035238; P:vitamin A biosynthetic process; IDA:FlyBase.
GO; GO:0009110; P:vitamin biosynthetic process; IMP:FlyBase.
InterPro; IPR004294; Carotenoid_Oase.
PANTHER; PTHR10543; PTHR10543; 1.
Pfam; PF03055; RPE65; 1.
1: Evidence at protein level;
Complete proteome; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
Reference proteome.
CHAIN 1 620 Carotenoid isomerooxygenase.
/FTId=PRO_0000424157.
METAL 211 211 Iron; catalytic. {ECO:0000250}.
METAL 267 267 Iron; catalytic. {ECO:0000250}.
METAL 337 337 Iron; catalytic. {ECO:0000250}.
METAL 612 612 Iron; catalytic. {ECO:0000250}.
MUTAGEN 280 280 E->K: In ninaB(P315); abolishes catalytic
activity. {ECO:0000269|PubMed:11158606}.
MUTAGEN 471 471 M->L: In ninaB(P315); no effect.
{ECO:0000269|PubMed:11158606}.
MUTAGEN 477 477 E->A: In ninaB(P315); no effect.
{ECO:0000269|PubMed:11158606}.
SEQUENCE 620 AA; 69932 MW; 91EC22EB102C31C3 CRC64;
MAAGVFKSFM RDFFAVKYDE QRNDPQAERL DGNGRLYPNC SSDVWLRSCE REIVDPIEGH
HSGHIPKWIC GSLLRNGPGS WKVGDMTFGH LFDCSALLHR FAIRNGRVTY QNRFVDTETL
RKNRSAQRIV VTEFGTAAVP DPCHSIFDRF AAIFRPDSGT DNSMISIYPF GDQYYTFTET
PFMHRINPCT LATEARICTT DFVGVVNHTS HPHVLPSGTV YNLGTTMTRS GPAYTILSFP
HGEQMFEDAH VVATLPCRWK LHPGYMHTFG LTDHYFVIVE QPLSVSLTEY IKAQLGGQNL
SACLKWFEDR PTLFHLIDRV SGKLVQTYES EAFFYLHIIN CFERDGHVVV DICSYRNPEM
INCMYLEAIA NMQTNPNYAT LFRGRPLRFV LPLGTIPPAS IAKRGLVKSF SLAGLSAPQV
SRTMKHSVSQ YADITYMPTN GKQATAGEES PKRDAKRGRY EEENLVNLVT MEGSQAEAFQ
GTNGIQLRPE MLCDWGCETP RIYYERYMGK NYRYFYAISS DVDAVNPGTL IKVDVWNKSC
LTWCEENVYP SEPIFVPSPD PKSEDDGVIL ASMVLGGLND RYVGLIVLCA KTMTELGRCD
FHTNGPVPKC LHGWFAPNAI


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