CRTDH_NONDD
ID CRTDH_NONDD Reviewed; 487 AA.
AC L7WC64;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=1-hydroxycarotenoid 3,4-desaturase {ECO:0000303|PubMed:26138397};
DE EC=1.3.99.27 {ECO:0000250|UniProtKB:Q7WT72};
DE AltName: Full=1'-hydroxy-gamma-carotene 3,4-desaturase {ECO:0000305};
DE AltName: Full=1-hydroxycarotenoid 3,4-dehydrogenase {ECO:0000250|UniProtKB:Q7WT72};
GN Name=crtD {ECO:0000303|PubMed:26138397};
GN OrderedLocusNames=DDD_2394 {ECO:0000312|EMBL:AGC77521.1};
OS Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS dokdonensis).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=592029 {ECO:0000312|Proteomes:UP000011173};
RN [1] {ECO:0000312|Proteomes:UP000011173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17205 / KCTC 12402 / DSW-6 {ECO:0000312|Proteomes:UP000011173};
RX PubMed=23292138; DOI=10.1093/gbe/evs134;
RA Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA Kim J.F.;
RT "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL Genome Biol. Evol. 5:187-187(2013).
RN [2] {ECO:0007744|PDB:4REP}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH FAD, AND SUBUNIT.
RX PubMed=26138397; DOI=10.1016/j.enzmictec.2015.05.005;
RA Ahn J.W., Kim K.J.;
RT "Crystal structure of 1'-OH-carotenoid 3,4-desaturase from Nonlabens
RT dokdonensis DSW-6.";
RL Enzyme Microb. Technol. 77:29-37(2015).
CC -!- FUNCTION: Catalyzes the introduction of a C-3,4 double bond into 1'-
CC hydroxy-gamma-carotene and rhodopin (1-hydroxylycopene) to yield 1'-
CC hydroxytorulene and (3E)-3,4-didehydrorhodopin, respectively (By
CC similarity). Can also use 1-hydroxy-all-trans-1,2-dihydro-neurosporene,
CC 1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene and 1,1'-dihydroxy-
CC 1,1',2,2'-tetrahydrolycopene (By similarity). Probably involved in the
CC synthesis of myxol, a gamma-carotene derivative (Probable). May use FAD
CC as a proton acceptor (Probable). {ECO:0000250|UniProtKB:Q7WT72,
CC ECO:0000305|PubMed:26138397}.
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:0000250|UniProtKB:Q7WT72};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-hydroxy-gamma-carotene + A = 1'-hydroxytorulene + AH2;
CC Xref=Rhea:RHEA:59332, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:80133, ChEBI:CHEBI:80134;
CC Evidence={ECO:0000250|UniProtKB:Q7WT72};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hydroxy-all-trans-1,2-dihydro-neurosporene + A = AH2 +
CC demethylspheroidene; Xref=Rhea:RHEA:59336, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:62505, ChEBI:CHEBI:138077;
CC Evidence={ECO:0000250|UniProtKB:Q7WT72};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene + A = 1'-
CC hydroxy-demethylspheroidene + AH2; Xref=Rhea:RHEA:59340,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:138076,
CC ChEBI:CHEBI:143013; Evidence={ECO:0000250|UniProtKB:Q7WT72};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene + A = 1,1'-
CC dihydroxy-3,4-didehydro-1,2-dihydrolycopene + AH2;
CC Xref=Rhea:RHEA:59444, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:63065, ChEBI:CHEBI:132450;
CC Evidence={ECO:0000250|UniProtKB:Q7WT72};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000255|RuleBase:RU362075}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26138397}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000255|RuleBase:RU362075}.
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DR EMBL; CP001397; AGC77521.1; -; Genomic_DNA.
DR RefSeq; WP_015363018.1; NC_020156.1.
DR PDB; 4REP; X-ray; 1.97 A; A=1-487.
DR PDBsum; 4REP; -.
DR AlphaFoldDB; L7WC64; -.
DR SMR; L7WC64; -.
DR STRING; 592029.DDD_2394; -.
DR EnsemblBacteria; AGC77521; AGC77521; DDD_2394.
DR KEGG; ndo:DDD_2394; -.
DR PATRIC; fig|592029.3.peg.2371; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019722_2_1_10; -.
DR OMA; FTMRWVF; -.
DR OrthoDB; 418913at2; -.
DR BRENDA; 1.3.99.27; 14193.
DR BRENDA; 1.3.99.37; 14193.
DR Proteomes; UP000011173; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; 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 3D-structure; Carotenoid biosynthesis; FAD; Flavoprotein;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..487
FT /note="1-hydroxycarotenoid 3,4-desaturase"
FT /id="PRO_0000447219"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23292138,
FT ECO:0007744|PDB:4REP"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23292138,
FT ECO:0007744|PDB:4REP"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23292138,
FT ECO:0007744|PDB:4REP"
FT BINDING 461
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT BINDING 468..469
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26138397,
FT ECO:0007744|PDB:4REP"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:4REP"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:4REP"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 303..313
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 382..401
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4REP"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:4REP"
FT HELIX 469..487
FT /evidence="ECO:0007829|PDB:4REP"
SQ SEQUENCE 487 AA; 54767 MW; D71FA01681C84674 CRC64;
MKNAIVIGAG IGGLAAALRL RHQGYSVTIF EKNDYAGGKL HAIEKDGYRF DLGPSLFTLP
HLVENLFALF PEEIIDFGYK SKAISFHYFW DDGTLFKAST DSSQFIEDAS KVFKEEKSTI
KKYLAKSKSK YELTKSLFLE KSLHKATTYF SLDTVKAIVH APFLGLNNTL NDENSKFKNP
KLTQLFNRYA TYNGSSPYQT PGIMTMIPHL ELGLGTYYPD GGMHRISQSL FELAQKVGVK
FRFRESVTNI TTSKNKVTGV ETKNGSYLSD LVVSNMDIVP TYRNLMKDVP APEKTLSQER
SSSALIFYWG IDREFPELDL HNILFSEDYK TEFEHIFEHK TLAQDPTVYI NITSKESSND
APAGHENWFV MINAPGDYGQ DWEQLVEESK KQIIAKIKKC LHVDISKHIT TEYILTPQGI
EKNTSSYRGA LYGAASNNKF AAFLRHPNFN GKIKNLYHVG GSVHPGGGIP LCLLSAQITA
DLIQKEQ
