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Database: UniProt
Entry: A0A425XY54_9BACT
LinkDB: A0A425XY54_9BACT
Original site: A0A425XY54_9BACT 
ID   A0A425XY54_9BACT        Unreviewed;       548 AA.
AC   A0A425XY54;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Sulfite reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DWB61_14260 {ECO:0000313|EMBL:RRG19711.1};
OS   Ancylomarina euxinus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Ancylomarina.
OX   NCBI_TaxID=2283627 {ECO:0000313|EMBL:RRG19711.1, ECO:0000313|Proteomes:UP000285794};
RN   [1] {ECO:0000313|EMBL:RRG19711.1, ECO:0000313|Proteomes:UP000285794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1P {ECO:0000313|EMBL:RRG19711.1,
RC   ECO:0000313|Proteomes:UP000285794};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Ancylomarina sp. M1P.";
RL   Submitted (JUL-2018) 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};
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:RRG19711.1}.
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DR   EMBL; QQWG01000017; RRG19711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A425XY54; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000285794; Unassembled WGS sequence.
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   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   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          25..163
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          185..399
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   548 AA;  62529 MW;  589C2753D47E271F CRC64;
     MTSYILKTKP KAFSIPNIKG ISSPITILYG GKSGNSAFIA EQMRCQFQTY ELEPAVYNMA
     EYDVNNLVNE KFIFIVVSTR GEGDPPAQAQ QFYKYLFGSK APKLPNLTFS VCALGDSSYQ
     YFCQAGKDID MKLKALGANR YSGLVTCDLA FNSKAEEWAS NLINKFQNRC NGDSLALKFG
     PNSIGPTFTL RVKDKYRITG EQSASEIHHL ILQTDHPDFT YQPGDSISIK PKNPYSLVVR
     IMIKQDYTPD LIVKYKEKNK SIEELLAVKL ELTKLGEDVL RAYQIYTGDE NLKELLEHKE
     DLFDYLKQAD VYDMLCDFPS QIEASKLSQI LTKIQLREYS ISSSLSETPN EVHLTVKQYN
     YSAFERERTG ACSSYINKGL QIDSSLKIQV IPNEEFRLPD DELPIIMIGS GTGIAPYMSF
     LKERRARVAS GDNWLIFGEK QEEYDFLYQN EIESLKAEGI LTRLDLAFSR DQAEKIYVQD
     RLKEKGREIF DWLEKGAHLF ICGSIAMGKD VKRNLIELIQ KDGIMDEVQA LAYFEHLEND
     SRYHEDVY
//
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