CRTU_CHLTE
ID CRTU_CHLTE Reviewed; 647 AA.
AC Q8KFK3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Carotenoid phi-ring synthase {ECO:0000305};
DE EC=1.3.99.39 {ECO:0000305|PubMed:15292122};
DE AltName: Full=Carotenoid beta-ring:acceptor oxidoreductase/methyltranferase (phi-ring forming) {ECO:0000305};
DE AltName: Full=Gamma-carotene desaturase {ECO:0000303|PubMed:15292122};
GN Name=crtU {ECO:0000303|PubMed:15292122};
GN OrderedLocusNames=CT0323 {ECO:0000312|EMBL:AAM71569.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=TLS / WT2321;
RX PubMed=15292122; DOI=10.1128/jb.186.16.5210-5220.2004;
RA Frigaard N.U., Maresca J.A., Yunker C.E., Jones A.D., Bryant D.A.;
RT "Genetic manipulation of carotenoid biosynthesis in the green sulfur
RT bacterium Chlorobium tepidum.";
RL J. Bacteriol. 186:5210-5220(2004).
CC -!- FUNCTION: Involved in the biosynthesis of chlorobactene, a carotenoid
CC with aromatic end group (PubMed:15292122). Catalyzes the introduction
CC of two additional double bonds into the ionone ring of gamma-carotene
CC to produce chlorobactene. The reaction includes an intramolecular
CC methyl transfer from position C1 to position C2 of the ring (Probable).
CC {ECO:0000269|PubMed:15292122, ECO:0000305|PubMed:15292122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + a carotenoid beta-end derivative = a carotenoid phi-end
CC derivative + 2 AH2; Xref=Rhea:RHEA:22524, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:139120, ChEBI:CHEBI:139129;
CC EC=1.3.99.39; Evidence={ECO:0000305|PubMed:15292122};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A2XDA1};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000269|PubMed:15292122}.
CC -!- DISRUPTION PHENOTYPE: Mutant lacks chlorobactene and all its
CC derivatives, and accumulates only gamma-carotene and its derivatives.
CC The growth rate of the mutant shows no significant deviation from the
CC wild-type growth rate at any light intensity.
CC {ECO:0000269|PubMed:15292122}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AE006470; AAM71569.1; -; Genomic_DNA.
DR RefSeq; NP_661227.1; NC_002932.3.
DR RefSeq; WP_010932015.1; NC_002932.3.
DR STRING; 194439.CT0323; -.
DR EnsemblBacteria; AAM71569; AAM71569; CT0323.
DR KEGG; cte:CT0323; -.
DR PATRIC; fig|194439.7.peg.313; -.
DR eggNOG; COG0723; Bacteria.
DR eggNOG; COG1232; Bacteria.
DR eggNOG; COG3349; Bacteria.
DR HOGENOM; CLU_026366_0_0_10; -.
DR OMA; HGFHGFF; -.
DR OrthoDB; 630753at2; -.
DR BioCyc; MetaCyc:MON-20348; -.
DR BRENDA; 1.3.99.39; 1345.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..647
FT /note="Carotenoid phi-ring synthase"
FT /id="PRO_0000453388"
FT DOMAIN 322..416
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 86..87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 362
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 364
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 380
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 383
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 601
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
FT BINDING 612
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A2XDA1"
SQ SEQUENCE 647 AA; 71204 MW; 63AD6171A3A772DC CRC64;
MQRREFFQHF LKRAGIGAGA LGAATAGLVG YYQPRKEVFD TSGKNNDELA EKLTTPKKAV
VIGGGLAGIS SALELARRNF EVTLVEASPS LGGKLTGWSI EALGEQFPVE HGFHGFFDQY
YNLNEMFASA GIGSDMFTAS PGYPVIFSDR QVEVFGQTPK WFPFNILSVV QQSKRLDIMS
FLKDYPGLWP VISMFRYQYD RTFRDWDSID FMTYCRRGEV LPAFIDTVLH PFSDATMNRM
EVLSAAEAMR YFHFYFMGSP EGLAFRIITK DCMSALIEPL ERKMTSLGVR VLKGRKAQNL
VMQDGRVTAV RLDGAGAANG EVASIPKREV PVTGWLQHMS DAGIPVLVAR RGASWVALDG
RCTHMGCPVA PEVSTGGFHC PCHDGRFNAE GLPVSGPPKA PLPRLDVREA GEMLVIGQAS
SSSSPVVVTA EELPCDYCVV ASGVRGTREL IALTRPGNSG FAGQVAALGE ADPYVVWRVW
LDRPLPSADF PFYTVSGYTY TDSITFYSSF QQPFIDWAKR TGGCVVELHA YAVAPQDVRP
EPEIRATMLQ ELHAMFPESK NATIRHEIFM MQSNFTRWAP GDHAKRPGVE TPYANLFLAG
DWVSTKAPVF LMEAAVFTGR MAANAISAKE SLRQKPLPIV PMNGIFA
