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Database: UniProt
Entry: A1SRM3_PSYIN
LinkDB: A1SRM3_PSYIN
Original site: A1SRM3_PSYIN 
ID   A1SRM3_PSYIN            Unreviewed;       740 AA.
AC   A1SRM3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ABM02138.1};
GN   OrderedLocusNames=Ping_0272 {ECO:0000313|EMBL:ABM02138.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02138.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02138.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02138.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP000510; ABM02138.1; -; Genomic_DNA.
DR   RefSeq; WP_011768697.1; NC_008709.1.
DR   AlphaFoldDB; A1SRM3; -.
DR   STRING; 357804.Ping_0272; -.
DR   KEGG; pin:Ping_0272; -.
DR   eggNOG; COG0369; Bacteria.
DR   eggNOG; COG3182; Bacteria.
DR   HOGENOM; CLU_001570_17_4_6; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000000639; Chromosome.
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; cd06201; SiR_like2; 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; 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; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 1.
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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..470
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          486..605
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   740 AA;  81723 MW;  CF8E1C343A6F4A07 CRC64;
     MLRKLHSYLG LAASILVVLL AISGAVLAIN PALDRAQAKV SGTDQISVAD VAANIARFYP
     NVEQLQRKAS GGLIVYYSNA NKAGADLVDP FTGEKIAAYS LSPFKRWVQN FHRSFLLDTP
     GRAAGGIGAL LMVVLSISGL FMLRTRQGGW RKIFRSMPGS IKQDLHGHFS RFAVLGLVLS
     AITGGYMSAN RFELIPVYQQ VDPAFPETVN GGKPAAVDAL PALQDIAFSD LRELVYPYAG
     DIRDVYSLRT DQGVGFIDQA TGELLSYQMY GTPQKIYEFI YMLHTGEGLW WLALLVGLAS
     FSVPLLAVTG LQIFMKRRRS IIRIKNNATA NSADIVILVG SESNSTWGFA KTLHDALSLS
     GYRVHSNSMN NIASTYPKAK QMFILTSTYG DGDAPASAKL FMNKIKRFAN NPNFQFCVLG
     FGDRTFDSYG QFALDVNNVL LNKGWNPLTN IDIIDKQSTQ AFNRWGTVVG SLMGLDLDLI
     YCPVHLNTQL LQLVDRVDYG AEVNAPTAIL RFIPAEKKTA TFFNKIRRKP RLPQFSAGDL
     VGILPTESDG ARFYSLASAS KNRQLEICVH QHPQGICSNY LHKLQLGECI KGFIRENPTF
     RPRLEQSSII LIGAGTGIAP LIGFIRNNHT CHPMRLYWGG RDPNSDFLYR AELEQYLQDK
     RLTELVTAFS RTEESCYVQD KVLADAPKIQ ALISEGAQIL VCGGRPMSKC VAAAITRVIS
     PLQITLQDLK EQGRYLEDVY
//
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