HPNR_METCA
ID HPNR_METCA Reviewed; 515 AA.
AC Q60AV6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hopanoid C-3 methylase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN Name=hpnR {ECO:0000303|PubMed:22826256};
GN OrderedLocusNames=MCA0738 {ECO:0000312|EMBL:AAU93108.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
RN [2]
RP FUNCTION IN METHYLATION OF HOPANOIDS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=22826256; DOI=10.1073/pnas.1208255109;
RA Welander P.V., Summons R.E.;
RT "Discovery, taxonomic distribution, and phenotypic characterization of a
RT gene required for 3-methylhopanoid production.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12905-12910(2012).
CC -!- FUNCTION: Required for methylation of hopanoids at the C-3 position.
CC {ECO:0000269|PubMed:22826256}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9X2H6};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q9X2H6};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant can produce both the desmethyl
CC aminobacteriohopanepentol and aminobacteriohopanetetrol but not their
CC C-3 methylated counterparts. Deletion results in reduced
CC intracytoplasmic membranes and in decreased survival in late stationary
CC phase. {ECO:0000269|PubMed:22826256}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; AE017282; AAU93108.1; -; Genomic_DNA.
DR RefSeq; WP_010960068.1; NC_002977.6.
DR AlphaFoldDB; Q60AV6; -.
DR SMR; Q60AV6; -.
DR STRING; 243233.MCA0738; -.
DR EnsemblBacteria; AAU93108; AAU93108; MCA0738.
DR KEGG; mca:MCA0738; -.
DR eggNOG; COG1032; Bacteria.
DR HOGENOM; CLU_021572_7_0_6; -.
DR OMA; HRRKYFI; -.
DR OrthoDB; 973846at2; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR027564; HpnR_B12_rSAM.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00565; hopanoid_C3-methyltransferase; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR04367; HpnR_B12_rSAM; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..515
FT /note="Hopanoid C-3 methylase"
FT /id="PRO_0000434049"
FT DOMAIN 8..141
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT DOMAIN 181..395
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
SQ SEQUENCE 515 AA; 58769 MW; 83CFD248D77C314F CRC64;
MKVFCVHPSP LMYTKVFLRL EPLGLELVAE SLRRAGHDIR LMDLQVESHA DFLRELDTWR
PDVVCFSLNY LANVPEVIDL AKTAKSRLPE CFTFVGGHSA SFVAKDLLDH GEGLLDCVLR
GEGEAGAPKL LETLARRGNI DEVPGVVSLT GEGPPPGFTD NLDEHLPARD LLKYRRKYFL
GTLDPCASIE FSRGCPWDCS FCSAWTFYGR SYRVMSTERI MEDLRRIKEP GIFIVDDVAF
IQAQHGMEIG EAIAREGIRK QYYLETRGDV LLRNKEVFKL WKKLGMEYMF LGVEAIDAEG
LQKFRKRVSL GKNFEALEFA RSLGITVAIN LIADPDWDRE RFEVIRQWCM EIPEIVNISV
NTPYPGTESW HTESRQLTTR DYRLFDIQHA VLPTRLPLPE FYGELVKTQQ VLYKKHMGWA
AARDTLKILG GHLLRGQTNF LRSLWKFNSV FNPELQLADH RQPVKYPMTL PPAPTEQKIE
AKTLYVHRSQ GRKSRALDDA TEKFVDEGRM GAATG
