CRTF_RHOCB
ID CRTF_RHOCB Reviewed; 393 AA.
AC D5AP78; P17061;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Demethylspheroidene O-methyltransferase;
DE EC=2.1.1.210;
DE AltName: Full=Hydroxyneurosporene methyltransferase;
GN Name=crtF; OrderedLocusNames=RCAP_rcc00685;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2747617; DOI=10.1007/bf00334364;
RA Armstrong G.A., Alberti M., Leach F., Hearst J.E.;
RT "Nucleotide sequence, organization, and nature of the protein products of
RT the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus.";
RL Mol. Gen. Genet. 216:254-268(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8468299; DOI=10.1128/jb.175.8.2407-2413.1993;
RA Burke D.H., Alberti M., Hearst J.E.;
RT "The Rhodobacter capsulatus chlorin reductase-encoding locus, bchA,
RT consists of three genes, bchX, bchY, and bchZ.";
RL J. Bacteriol. 175:2407-2413(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=12770713; DOI=10.1016/s0378-1097(03)00302-1;
RA Badenhop F., Steiger S., Sandmann M., Sandmann G.;
RT "Expression and biochemical characterization of the 1-HO-carotenoid
RT methylase CrtF from Rhodobacter capsulatus.";
RL FEMS Microbiol. Lett. 222:237-242(2003).
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. {ECO:0000269|PubMed:12770713}.
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 Evidence={ECO:0000269|PubMed:12770713};
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; X52291; CAA36539.1; -; Genomic_DNA.
DR EMBL; Z11165; CAA77546.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84450.1; -; Genomic_DNA.
DR PIR; S04408; S04408.
DR RefSeq; WP_013066429.1; NC_014034.1.
DR AlphaFoldDB; D5AP78; -.
DR SMR; D5AP78; -.
DR STRING; 272942.RCAP_rcc00685; -.
DR EnsemblBacteria; ADE84450; ADE84450; RCAP_rcc00685.
DR GeneID; 31489631; -.
DR KEGG; rcp:RCAP_rcc00685; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_005533_12_0_5; -.
DR OMA; EYMEGFL; -.
DR OrthoDB; 1213908at2; -.
DR UniPathway; UPA00683; -.
DR Proteomes; UP000002361; Chromosome.
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; 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; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chlorophyll biosynthesis; Methyltransferase;
KW Photosynthesis; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..393
FT /note="Demethylspheroidene O-methyltransferase"
FT /id="PRO_0000410434"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 393 AA; 43039 MW; 166FB8A80C88F393 CRC64;
MPKDDHTGAT ADRTAQPTGT GKQPLVPGQP GAAPVQPGRV NFFTRIALSQ RLHEIFERLP
LMNRVTRREG EALFDIVSGF VQSQVLLAIV EFRVLHILAG ASWPLPQLAE RTGLAEDRLA
VLMQAAAALK LVKFRRGLWQ LAPRGAAFIT VPGLEAMVRH HPVLYRDLAD PVAFLKGDIE
PELAGFWPYV FGPLAQEDAG LAERYSQLMA DSQRVVADDT LRLVDLRDAK RVMDVGGGTG
AFLRVVAKLY PELPLTLFDL PHVLSVADRF SPKLDFAPGS FRDDPIPQGA DVITLVRVLY
DHPDSVVEPL LAKVHAALPP GGRLIISEAM AGGAKPDRAC DVYFAFYTMA MSSGRTRSPE
EIKQMLEKAG FTKVSKPRTL RPFITSVIEA ERG
