ID A0A0A1VCZ9_9BURK Unreviewed; 462 AA.
AC A0A0A1VCZ9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Sulfite reductase, alpha subunit {ECO:0000313|EMBL:GAD21029.1};
GN ORFNames=AVS7_00790 {ECO:0000313|EMBL:GAD21029.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD21029.1};
RN [1] {ECO:0000313|EMBL:GAD21029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD21029.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; DF238897; GAD21029.1; -; Genomic_DNA.
DR RefSeq; WP_020230384.1; NZ_DF238897.1.
DR AlphaFoldDB; A0A0A1VCZ9; -.
DR STRING; 1268622.AVS7_00790; -.
DR eggNOG; COG0369; Bacteria.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000030646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06200; SiR_like1; 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; 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; 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; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030646};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..194
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 211..322
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 462 AA; 49665 MW; B26CBABC56494EDA CRC64;
MAFSESALRM AAAVLLIVLY AALCGGIWLR QRRQQARARQ EAAVLASARD GVQPLLIAFA
SQTGQAEELA RETARLLHTA GEPVHLCALN AVDAALLART QRALFVASTY GEGDAPDNAA
LFQSRCMGEG AVGALDHLHF GLLALGDRQY AQFCGFGRAL DAWLQARGAV PWFERIDMDN
AAPAALAAWQ HHLAQVSSLS EVPALDAWQA GAFEPWTLAE RRHLNPGSAG APVFHLALQP
PRGDAAWESG DLAQVRVPAA PEHPREYSIA SIAADGRVHL LVRQALREDG TPGVASGWLT
QEAPLGGAVE VRLRAHRNFR LEDNAARPLV LIGNGTGLAG LRGHLRARAA AGAGPNWLLF
GERNAAHDTL YGDELQAWLT SGVLQRLDLA FSRDQAVCVY VQDRLAQAAD TLREWVQGGA
AIYVCGSLQG MAQGVDDTLR AVLGAEQMEQ LVRSGRYRRD VY
//
