ID I3ZE55_TERRK Unreviewed; 585 AA.
AC I3ZE55;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Sulfite reductase, alpha subunit (Flavoprotein) {ECO:0000313|EMBL:AFL87523.1};
GN OrderedLocusNames=Terro_1213 {ECO:0000313|EMBL:AFL87523.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL87523.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL87523.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP003379; AFL87523.1; -; Genomic_DNA.
DR RefSeq; WP_014785092.1; NC_018014.1.
DR AlphaFoldDB; I3ZE55; -.
DR STRING; 926566.Terro_1213; -.
DR KEGG; trs:Terro_1213; -.
DR PATRIC; fig|926566.3.peg.1193; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_001570_17_7_0; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000006056; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; 3.40.50.360; -; 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; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
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; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 43..181
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 217..435
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 585 AA; 64346 MW; 78BB84F4C911920B CRC64;
MSVPFLPDNA PFSTEQRAWL NGFLAGLFSA APTAAAAVDP LQLAVYFASQ SGTAERLAKK
LVKELKAQGH VAELASLAKV TLADVAGKQH ALFLVSTYGE GDPPESSISF RDSLFADGAP
KLDAMRYAVF ALGDRHYEQF CKFGADVDER LRALGATRLM ARVDADVDVD VPFEQWKTAL
RPHLTQAQVP GVVASTAPVA VACAAESAPA SPGHSRDNPF HAEMRERKPL TRDVSSKMTM
HLSFGLADSD VHYQAGDACG VIAQNDPELV EEILTLLPFA ADTKIEVAKS GVTTVRDALL
HHLQPTRLTR KIVQHFAART EAKPLTTLLL PEEASHLDSF MWDRGLVDLL HEYPGSVSEP
AELVSMLPRL SPRLYSISSS PAAHGREVHC TIAVVRYRSH NRERGGIAST MLSDRVRVGE
RLPIYIQPNK KFRLPASDVP MIMIGPGTGI APFRAFLHER QALGHGGRNW LFFGERSAQT
DFLYCDELHG LRDSGYLTRL DTAFSRDQSH KIYVQDRMKE NGAELWRWLC EGAQIYVCGD
ASRMAKDVDA SLHEVIARHG GMNAEAAGDY VSQLHDDGRY HRDVY
//
