ID R7WLV7_9NOCA Unreviewed; 383 AA.
AC R7WLV7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Sulfite reductase [NADPH] flavoprotein {ECO:0000313|EMBL:EOM74999.1};
GN ORFNames=Rrhod_3612 {ECO:0000313|EMBL:EOM74999.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM74999.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM74999.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM74999.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOM74999.1}.
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DR EMBL; APMY01000109; EOM74999.1; -; Genomic_DNA.
DR RefSeq; WP_010839640.1; NZ_APMY01000109.1.
DR AlphaFoldDB; R7WLV7; -.
DR PATRIC; fig|1273125.3.peg.3440; -.
DR eggNOG; COG0369; Bacteria.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000013525; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06199; SiR; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 2.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525}.
FT DOMAIN 19..231
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 383 AA; 41714 MW; F4D5B1369FA3F1E7 CRC64;
MTSAVRRSAR ASRSPWNRKN PFAARVVTST RLTGPGSSKD VRHHVLDLAD SGIEYEPGDG
LGIHPVNDPA LVDAVLTRLG ASPEAVVAGY ELPLADVLRT RRELTLPSRD LLEYVATHGG
PPELLDIAAD RTTRELWRRG KDAADVLDLL PSPPSVEEFV ALAGPLAHRT YSISSAPSVH
PGVVHLTVST VRGAATDRPR SGACSTHLAD RLGESGEAAI FLVRNKSFRL PADDAAPVIM
IGPGTGVAPF RAFLQERDAR GATGGAWLFY GDRTREHDFL YRDEFADFRD RGVLTELDLA
FSRDGDPTAK QYVQHRMRER GDELVAWLDR GAHLYVCGDT TMATDVDDTL VSLVAEHRGA
TPGAASDYVA DLRTTKRYVR DVY
//
