NINAB_GALME
ID NINAB_GALME Reviewed; 513 AA.
AC A8Y9I2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Carotenoid isomerooxygenase;
DE EC=1.13.11.65;
DE AltName: Full=Beta-carotene 15,15'-monooxygenase and retinoid isomerase;
DE AltName: Full=Beta-carotene dioxygenase and retinoid isomerase;
DE AltName: Full=Neither inactivation nor afterpotential mutant B;
GN Name=ninaB;
OS Galleria mellonella (Greater wax moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Galleriinae; Galleria.
OX NCBI_TaxID=7137;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Pupae;
RX PubMed=19020100; DOI=10.1073/pnas.0807805105;
RA Oberhauser V., Voolstra O., Bangert A., von Lintig J., Vogt K.;
RT "NinaB combines carotenoid oxygenase and retinoid isomerase activity in a
RT single polypeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19000-19005(2008).
CC -!- FUNCTION: Catalyzes the oxidative cleavage at the 15,15'-double bond of
CC carotenoids and the simultaneous all-trans to 11-cis isomerization of
CC one cleavage product. Carotenoids like 11-cis retinal can promote
CC visual pigment biogenesis in the dark. Essential for the biosynthesis
CC of the 3-hydroxyretinal chromophore of rhodopsin from zeaxanthin and
CC for proper photoreceptor development. {ECO:0000269|PubMed:19020100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal +
CC (3R)-all-trans-3-hydroxyretinal; Xref=Rhea:RHEA:33931,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:52228,
CC ChEBI:CHEBI:66898; EC=1.13.11.65;
CC Evidence={ECO:0000269|PubMed:19020100};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AM778534; CAO85888.1; -; mRNA.
DR AlphaFoldDB; A8Y9I2; -.
DR SMR; A8Y9I2; -.
DR KEGG; ag:CAO85888; -.
DR BRENDA; 1.13.11.65; 2389.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000504614; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004294; Carotenoid_Oase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..513
FT /note="Carotenoid isomerooxygenase"
FT /id="PRO_0000424158"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 57839 MW; 4077733AF2E73962 CRC64;
MAVHQEKLYP NCDSGVWLRS CEEEVTEPLE GTITGEIPSW LQGSLLRNGP GSLKVGSMRF
EHLFDSSALL HRFAINDGSV TYQCRFLQSN TFKKNRAAER IVVTEFGTRA VPDPCHTIFD
RVAALFKPGE SLSDNAMISL YPFGDEIYAF TEGPVIHRID PETLDTLERR NLMDSVSLVN
HTSHPHVMPN GDVYNLGMSI VQGRLKHVIV KFPYTEKGDM FAKAHIVANM SPRWPLHPAY
MHTFGITENY FVIVEQPLSV SLLTMVKSQP SNEPLASSLH WYPNHETHIV LLSRRDGKEV
KRYRTEPLFY LHIINAYEHD GVLVVDLCAY KDAKAIDAMY INAIETMQSN ADYAEWFRGR
PKRLELPLNA TNCSRIEPRL LAQLGCETPR IHYDLYNGRP YRYFYAISSD VDAANPGTII
KVDTKTGETK TWCDTNCYPS EPIFVPAPGA TEEDDGVILS ALVWGGAGAH CRRVALLVLE
ARGLRELARA TFCAPSPVPK CLHGWFLPRR TQL