RTXC_BRAEL
ID RTXC_BRAEL Reviewed; 352 AA.
AC Q93HS4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Dihydrorhizobitoxine desaturase {ECO:0000303|PubMed:11679318};
DE EC=1.14.19.61 {ECO:0000305|PubMed:11679318, ECO:0000305|PubMed:14711685};
GN Name=rtxC {ECO:0000303|PubMed:11679318};
GN ORFNames=BEL01nite_69950 {ECO:0000312|EMBL:GEC57952.1},
GN FBF72_28720 {ECO:0000312|EMBL:NWL71962.1},
GN JOH49_009324 {ECO:0000312|EMBL:MBP1299571.1};
OS Bradyrhizobium elkanii.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=29448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=USDA94;
RX PubMed=11679318; DOI=10.1128/aem.67.11.4999-5009.2001;
RA Yasuta T., Okazaki S., Mitsui H., Yuhashi K., Ezura H., Minamisawa K.;
RT "DNA sequence and mutational analysis of rhizobitoxine biosynthesis genes
RT in Bradyrhizobium elkanii.";
RL Appl. Environ. Microbiol. 67:4999-5009(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SEMIA 587;
RA Ambrosini A., Guzman F., Sant'Anna F.H., Passaglia L.M.P.;
RT "Genome of Bradyrhizobium elkanii SEMIA 587.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 14791;
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Bradyrhizobium elkanii NBRC 14791.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA 406;
RA Whitman W., Huntemann M., Clum A., Spunde A., Palaniappan K., Ritter S.,
RA Mikhailova N., Chen I.-M., Stamatis D., Reddy T., O'Malley R., Daum C.,
RA Shapiro N., Ivanova N., Kyrpides N., Woyke T.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=USDA94;
RX PubMed=14711685; DOI=10.1128/aem.70.1.535-541.2004;
RA Okazaki S., Sugawara M., Minamisawa K.;
RT "Bradyrhizobium elkanii rtxC gene is required for expression of symbiotic
RT phenotypes in the final step of rhizobitoxine biosynthesis.";
RL Appl. Environ. Microbiol. 70:535-541(2004).
CC -!- FUNCTION: Involved in the biosynthesis of the nodulation enhancer
CC compound rhizobitoxine. Catalyzes the final step of the pathway, the
CC introduction of a carbon double bond into the C3 position of
CC dihydrorhizobitoxine to produce rhizobitoxine.
CC {ECO:0000269|PubMed:11679318, ECO:0000269|PubMed:14711685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydrorhizobitoxine + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin] +
CC rhizobitoxine; Xref=Rhea:RHEA:56684, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:140641,
CC ChEBI:CHEBI:140642; EC=1.14.19.61;
CC Evidence={ECO:0000305|PubMed:11679318, ECO:0000305|PubMed:14711685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56685;
CC Evidence={ECO:0000305|PubMed:11679318, ECO:0000305|PubMed:14711685};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant can produce serinol and
CC dihydrorhizobitoxine, but not rhizobitoxine (PubMed:11679318,
CC PubMed:14711685). Mutant produces no symptoms of foliar chlorosis on G.
CC max cv. Lee and does not accumulate rhizobitoxine in the nodules or
CC upper shoots (PubMed:14711685). It shows significantly less nodulation
CC competitiveness than the wild-type strain on M. atropurpureum
CC (PubMed:14711685). {ECO:0000269|PubMed:11679318,
CC ECO:0000269|PubMed:14711685}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB062279; BAB55901.1; -; Genomic_DNA.
DR EMBL; BJNL01000074; GEC57952.1; -; Genomic_DNA.
DR EMBL; SWAO01000075; NWL71962.1; -; Genomic_DNA.
DR EMBL; JAFICZ010000001; MBP1299571.1; -; Genomic_DNA.
DR RefSeq; WP_016841944.1; NZ_SEMA01000031.1.
DR GeneID; 66429291; -.
DR KEGG; ag:BAB55901; -.
DR BioCyc; MetaCyc:MON-20271; -.
DR BRENDA; 1.14.19.61; 9755.
DR Proteomes; UP000315237; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Dihydrorhizobitoxine desaturase"
FT /id="PRO_0000454506"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 40461 MW; 7C4F6FE5F9DC19A3 CRC64;
MNQADAWKLR SSRYEAVQFS REINKQLSEL RPDNVMGAIY IAKDYAVIAA CTLATLCVSW
WLYPLAVLLI GAYQRGLTTI AHDAAHRTLA KNTTWNYVLG ILFAAYPLFQ RHWAYRISHV
YLHHPYLGDP EKDPDLKFFM ANGVYDVQPP KRYAFNIIWK PIFGGATLAY LKYLWTNRFS
ITDSEDQSRS SILVDKYGFY LFWIGILAGS YALGLLHIVI LFWIVPYLTT FQVLGWFVEL
AEHSPMCESE TKNVYLTRNR KGNFLERAIL GQNLDEYHLE HHLSPGIPFW LLHKAQKIRM
QDPGYAKVAA SWGGLFVKGP QGQPSVITQL KERNRRLYEQ SLADAHAKGH VA
