CRTF_CERS4
ID CRTF_CERS4 Reviewed; 379 AA.
AC P54906; Q3J196; Q9RFC4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Demethylspheroidene O-methyltransferase;
DE EC=2.1.1.210;
DE AltName: Full=Hydroxyneurosporene methyltransferase;
GN Name=crtF; OrderedLocusNames=RHOS4_18700; ORFNames=RSP_0264;
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=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 [2]
RP SEQUENCE REVISION TO 373.
RA Naylor G.W.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [4]
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.
CC -!- FUNCTION: Methyltransferase that mediates the O-methylation of 1-
CC hydroxy carotenoids. Converts hydroxyneurosporene to
CC methoxyneurosporene or demethylspheroidene to spheroidene. Also able to
CC produce spirilloxanthin (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=demethylspheroidene + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + spheroidene; Xref=Rhea:RHEA:30903,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:35330, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:62505; EC=2.1.1.210;
CC -!- PATHWAY: Carotenoid biosynthesis; spheroidene biosynthesis.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AJ010302; CAB38745.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24295.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79438.1; -; Genomic_DNA.
DR PIR; T50751; T50751.
DR RefSeq; WP_011338111.1; NZ_CP030271.1.
DR RefSeq; YP_353339.1; NC_007493.2.
DR AlphaFoldDB; P54906; -.
DR SMR; P54906; -.
DR STRING; 272943.RSP_0264; -.
DR EnsemblBacteria; ABA79438; ABA79438; RSP_0264.
DR KEGG; rsp:RSP_0264; -.
DR PATRIC; fig|272943.9.peg.2208; -.
DR eggNOG; COG0500; Bacteria.
DR OMA; EYMEGFL; -.
DR PhylomeDB; P54906; -.
DR UniPathway; UPA00683; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0043803; F:hydroxyneurosporene-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF16864; Dimerisation2; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis; Chlorophyll biosynthesis; Methyltransferase;
KW Photosynthesis; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..379
FT /note="Demethylspheroidene O-methyltransferase"
FT /id="PRO_0000079368"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT CONFLICT 18..23
FT /note="GVRLAG -> APLP (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> G (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Missing (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Q -> H (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> F (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="TR -> KP (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..113
FT /note="DG -> QR (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..120
FT /note="DLAVR -> HLGGP (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="LE -> VQ (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> W (in Ref. 3; AAF24295)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> E (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..329
FT /note="FY -> GD (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="EL -> DV (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="F -> G (in Ref. 1; CAB38745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 40788 MW; 4D66C754EDC0A3C1 CRC64;
MSALRPPARG GLGLSRLGVR LAGSRRFQLI AERVPFLRRI GRREGEELFD IVAGFVHSQV
LYALVELRVL HLVAEGPQTV QALAAATGLA PERMQLLLQG GAALKLLTRR RDGQFDLAVR
GAAFLAVPGL EAMVGHHHVL YRDLADPVAF LKGETEPELA RFWPYVFGAG GATDPEVTAK
YSRLMTESQG LVAEDALRLV DLMGVRRLMD VGGGTGAFLA AVGRAYPLME LMLFDLPVVA
EAAPQRLTEA GLAGRFTVHG GSFRDDPLPL GADAISLVRV LFDHSDETVK LLLHRVREAL
PAGGRVIVAE AMSGGARPHR ETDTYMAFYT AAMRTGRVRS AAEIAELLTG QGFSEIKIFP
GLRPYVASAV TAVRPSDAP
