CRTD_CERS4
ID CRTD_CERS4 Reviewed; 495 AA.
AC Q01671; Q3J194;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 25-MAY-2022, entry version 137.
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; OrderedLocusNames=RHOS4_18720; ORFNames=RSP_0266;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1612412; DOI=10.1016/0378-1097(92)90497-c;
RA Gari E., Toledo J.C., Gibert I., Barbe J.;
RT "Nucleotide sequence of the methoxyneurosporene dehydrogenase gene from
RT Rhodobacter sphaeroides: comparison with other bacterial carotenoid
RT dehydrogenases.";
RL FEMS Microbiol. Lett. 72:103-108(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7721699; DOI=10.1128/jb.177.8.2064-2073.1995;
RA Lang H.P., Cogdell R.J., Takaichi S., Hunter C.N.;
RT "Complete DNA sequence, specific Tn5 insertion map, and gene assignment of
RT the carotenoid biosynthesis pathway of Rhodobacter sphaeroides.";
RL J. Bacteriol. 177:2064-2073(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=9393712; DOI=10.1128/jb.179.23.7462-7467.1997;
RA Albrecht M., Ruther A., Sandmann G.;
RT "Purification and biochemical characterization of a hydroxyneurosporene
RT desaturase involved in the biosynthetic pathway of the carotenoid
RT spheroidene in Rhodobacter sphaeroides.";
RL J. Bacteriol. 179:7462-7467(1997).
CC -!- FUNCTION: Catalyzes the introduction of C-3,4 double bonds into 1-
CC hydroxyneurosporene (1-HO-Neu) to yield demethylspheroidene (DMS). It
CC prefer the acyclic carotenoids such as 1-hydroxylycopene, and 1-
CC hydroxy-gamma-carotene, whereas 1-hydroxy-3,4-didehydrolycopene and
CC 1,1-dihydroxylycopene are much less effective.
CC {ECO:0000269|PubMed:9393712}.
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:9393712};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.4 uM for hydroxyneurosporene (at pH 30 degrees Celsius and pH
CC 8) {ECO:0000269|PubMed:9393712};
CC -!- PATHWAY: Carotenoid biosynthesis; spheroidene biosynthesis.
CC -!- MISCELLANEOUS: The hydrogen acceptor in the C-3,4 desaturation reaction
CC is molecular oxygen. NAD, NADP, and FAD have no influence on enzymatic
CC activity. Another unknown electron acceptor may exist in Rhodobacter
CC species that replaces molecular oxygen during anaerobic growth
CC (PubMed:9393712). {ECO:0000305|PubMed:9393712}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; X63204; CAA44886.1; -; Genomic_DNA.
DR EMBL; AJ010302; CAB38743.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000143; ABA79440.1; -; Genomic_DNA.
DR PIR; S23633; S23633.
DR RefSeq; WP_011338113.1; NZ_CP030271.1.
DR RefSeq; YP_353341.1; NC_007493.2.
DR AlphaFoldDB; Q01671; -.
DR SMR; Q01671; -.
DR STRING; 272943.RSP_0266; -.
DR EnsemblBacteria; ABA79440; ABA79440; RSP_0266.
DR KEGG; rsp:RSP_0266; -.
DR PATRIC; fig|272943.9.peg.2210; -.
DR eggNOG; COG1233; Bacteria.
DR OMA; FTMRWVF; -.
DR PhylomeDB; Q01671; -.
DR SABIO-RK; Q01671; -.
DR UniPathway; UPA00683; -.
DR Proteomes; UP000002703; Chromosome 1.
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 InterPro; IPR008150; Phytoene_DH_bac_CS.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chlorophyll biosynthesis; Oxidoreductase;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..495
FT /note="Hydroxyneurosporene desaturase"
FT /id="PRO_0000067684"
FT CONFLICT 115
FT /note="A -> G (in Ref. 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="R -> P (in Ref. 1; CAA44886 and 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> P (in Ref. 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> M (in Ref. 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> G (in Ref. 1; CAA44886 and 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> P (in Ref. 1; CAA44886 and 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> I (in Ref. 2; CAB38743)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..443
FT /note="PHGA -> ATGP (in Ref. 1; CAA44886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 53033 MW; 834DAE05F629316F CRC64;
MRQIVPKVVV VGAGMGGLAS AIRLARAGCE VTLLEAREAP GGRMRTLPSV AGPVDAGPTV
LTLREVFDDI FEVCGQKLDH HLTLLPQPLL ARHWWLDGST LDLTTDLEAN VEAVAAFAGA
REARAFRRFH DLSARLYDAF DRPMMRAARP DLRAIATGAL KAPRTWPALL PGMTLDRLLR
LFFRDRRLRQ LFGRYATYVG GTPYGAPGVL ALIWAAEARG VWAIEGGMHR LALALARLAD
DQGVRLRYGA PVARILRQGG RATGVQLADG RTLPADHIVF NGDPAALLAG CLGDGPQDAV
PEDRIHPRSL SAWVWSYAAR ASGPPLVHHN VFFADDPRRE FGPIAAGQMP EDATLYICAE
DRSGGQLPDG PERFEIIMNG PPGRPAKPED FAQCRSRTFD RLRQFGLTFD PVPGETSLTA
PSGFASLFPA SQGSIYGLSP HGALASLKRP LARTALPGLW LAGGGAHPGA GVPMAALSGR
HAAEAILADL ASRSR
