CRTD_RUBGE
ID CRTD_RUBGE Reviewed; 525 AA.
AC Q9JPB5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Hydroxyneurosporene desaturase;
DE Short=HND;
DE AltName: Full=1-hydroxycarotenoid 3,4-dehydrogenase;
DE AltName: Full=1-hydroxycarotenoid 3,4-desaturase;
DE EC=1.3.99.27;
GN Name=crtD;
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RA Nagashima K.V., Shimada K., Matsuura K.;
RT "Phylogenetic analysis of photosynthetic genes of Rhodocyclus gelatinosus:
RT Possibility of horizontal gene transfer in purple bacteria.";
RL Photosyn. Res. 36:185-191(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=8300574; DOI=10.1016/s0021-9258(17)41970-3;
RA Nagashima K.V.P., Matsuura K., Ohyama S., Shimada K.;
RT "Primary structure and transcription of genes encoding B870 and
RT photosynthetic reaction center apoproteins from Rubrivivax gelatinosus.";
RL J. Biol. Chem. 269:2477-2484(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RX PubMed=10563807; DOI=10.1021/bi991146h;
RA Menin L., Yoshida M., Jaquinod M., Nagashima K.V., Matsuura K., Parot P.,
RA Vermeglio A.;
RT "Dark aerobic growth conditions induce the synthesis of a high midpoint
RT potential cytochrome c8 in the photosynthetic bacterium Rubrivivax
RT gelatinosus.";
RL Biochemistry 38:15238-15244(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144;
RA Igarashi N., Harada J., Nagashima S., Matsuura K., Shimada K.,
RA Nagashima K.V.P.;
RT "Horizontal transfer of the photosynthesis gene cluster and operon
RT rearrangement in purple bacteria.";
RL J. Mol. Evol. 52:333-341(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=10880364; DOI=10.1042/0264-6021:3490635;
RA Steiger S., Astier C., Sandmann G.;
RT "Substrate specificity of the expressed carotenoid 3,4-desaturase from
RT Rubrivivax gelatinosus reveals the detailed reaction sequence to
RT spheroidene and spirilloxanthin.";
RL Biochem. J. 349:635-640(2000).
CC -!- FUNCTION: Catalyzes the introduction of C-3,4 double bonds into 1-
CC hydroxyneurosporene (1-HO-Neu) to yield demethylspheroidene (DMS). The
CC preferred substrates are 1-hydroxy-neurosporene, 1-hydroxy-lycopene and
CC 1,1-dihydroxyneurosporene, however the 3,4-didehydrolycopene
CC derivatives such as 1,1-dihydroxy-3,4-didehydrolycopene, 1-methoxy-1-
CC hydroxy-3,4-didehydrolycopene and 1-hydroxy-3,4-didehydrolycopene are
CC also efficiently converted. 1-HO-carotene derivatives can be also used.
CC {ECO:0000269|PubMed:10880364}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + rhodopin = (3E)-3,4-didehydrorhodopin + AH2;
CC Xref=Rhea:RHEA:30919, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:35331, ChEBI:CHEBI:62481; EC=1.3.99.27;
CC Evidence={ECO:0000269|PubMed:10880364};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for 1,1-dihydroxneurosporene (at pH 28 degrees Celsius)
CC {ECO:0000269|PubMed:10880364};
CC KM=25 uM for 1-hydroxyneurosporene (at pH 28 degrees Celsius)
CC {ECO:0000269|PubMed:10880364};
CC KM=40 uM for 1-hydroxylycopene (at pH 28 degrees Celsius)
CC {ECO:0000269|PubMed:10880364};
CC Vmax=1.35 nmol/h/mg enzyme with 1-hydroxyneurosporene as substrate
CC (at pH 28 degrees Celsius) {ECO:0000269|PubMed:10880364};
CC Vmax=0.58 nmol/h/mg enzyme with 1,1-dihydroxneurosporene as substrate
CC (at pH 28 degrees Celsius) {ECO:0000269|PubMed:10880364};
CC Vmax=0.69 nmol/h/mg enzyme with 1-hydroxylycopene as substrate (at pH
CC 28 degrees Celsius) {ECO:0000269|PubMed:10880364};
CC -!- PATHWAY: Carotenoid biosynthesis; spheroidene biosynthesis.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AB034704; BAA94046.1; -; Genomic_DNA.
DR PIR; T50893; T50893.
DR AlphaFoldDB; Q9JPB5; -.
DR SMR; Q9JPB5; -.
DR OMA; FTMRWVF; -.
DR BRENDA; 1.3.99.37; 5401.
DR UniPathway; UPA00683; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW Photosynthesis.
FT CHAIN 1..525
FT /note="Hydroxyneurosporene desaturase"
FT /id="PRO_0000423971"
SQ SEQUENCE 525 AA; 56671 MW; B2927BE8552CE9E9 CRC64;
MAEPLRTHRV VVVGAGIAGL TSALLLAARG LDVTLVDKAA TPGGKMRQVM VDGAPVDAGP
TVFTMRWVFD QIFAAAGATV EEHLKLQPLG VLARHAWRGH EPRLDLFADI RRSAEAIGEF
SGPQEAQRFL GFCRQARQLY DHLEGPYIRS ERPTLGSMVG DLGPRGLMAL MQIGPFSNLW
RSLSRHFRDP KLQQLFARYA TYCGASPWMA PATLMLVAQV ELDGVWAVEG GMHAVAKAFS
ALAEARGVKT RYGCGCEQIL VRDGRAVGVR LAGGEEITAD SVVFNGDVNA LAQGLLGDPP
RRATAAVAPA RRSLSALTWL VNARTSGFPL VRHNVFFDED YASEFDDIFR QRQLPRRGTV
YVCAQDRTDE GIGSDAPERL LCLVNAPADG DRRPFDHSET DPCEQRSLAL MRECGLTIDW
SPQTHRLVTP ANFERLFPAT GGALYGPATH GWMSSFHRAS STSRLPGLYL AGGSVHPGPG
VPMAAMSGRL AAETLMAHLD STSRSRRVVI SGGMSTRSAT TGGMA
