位置:首页 > 蛋白库 > NINAB_GALME
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024