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Database: UniProt
Entry: A0A1S2QND2_9BACI
LinkDB: A0A1S2QND2_9BACI
Original site: A0A1S2QND2_9BACI 
ID   A0A1S2QND2_9BACI        Unreviewed;       390 AA.
AC   A0A1S2QND2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=BIV60_26990 {ECO:0000313|EMBL:OIK07668.1};
OS   Bacillus sp. MUM 116.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK07668.1, ECO:0000313|Proteomes:UP000180019};
RN   [1] {ECO:0000313|EMBL:OIK07668.1, ECO:0000313|Proteomes:UP000180019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUM 116 {ECO:0000313|EMBL:OIK07668.1,
RC   ECO:0000313|Proteomes:UP000180019};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Bacillus sp. MUM 116.";
RL   Submitted (OCT-2016) 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:OIK07668.1}.
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DR   EMBL; MLYR01000161; OIK07668.1; -; Genomic_DNA.
DR   RefSeq; WP_071358742.1; NZ_MLYR01000161.1.
DR   AlphaFoldDB; A0A1S2QND2; -.
DR   STRING; 1678002.BIV60_26990; -.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000180019; 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; 1.
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:UP000180019};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          20..239
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  43622 MW;  C17B179B64FEB4D4 CRC64;
     MQVTAENAKK DKPTPAFSRT NPFPAKVLKN VNLNGEGSSK ETRHLELSLE GSGLSYVPGD
     ALGVVPENDP ELVAALIEEM HWDGQAVVTI NKQGETLPLK EALTTFFEIT LLNKKILQQS
     ASFTENEALQ NLVLVENAAQ LKEYCYGRDL LDMLRDFGPW KASSQEIVSL LRKMPPRLYS
     IASSFTAHPG EVHLTIGAVR YTSNGRDRKG VCSVLCAERL KDGDTIPVFV QPNKHFHLSE
     SGESDIIMVG PGTGIAPFRS FIEERAVNKA TGRTWLFFGD QHAATDFLYQ SELEKYQQEG
     AVTKLDTAFS RDSEKKVYVQ HKMLENSQEL FAWLEKGAIF YVCGDKEHMA KDVHEALITV
     IEKEGARARD AAEAYLKDMQ QNGRYQRDVY
//
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