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Database: UniProt
Entry: A0A136HUL1_9ALTE
LinkDB: A0A136HUL1_9ALTE
Original site: A0A136HUL1_9ALTE 
ID   A0A136HUL1_9ALTE        Unreviewed;       460 AA.
AC   A0A136HUL1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Nitric oxide synthase {ECO:0000313|EMBL:KXJ59346.1};
GN   ORFNames=AXW14_05945 {ECO:0000313|EMBL:KXJ59346.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ59346.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:KXJ59346.1}.
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DR   EMBL; LSMP01000218; KXJ59346.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136HUL1; -.
DR   Proteomes; UP000070342; 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   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
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; 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; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..187
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   460 AA;  49708 MW;  DC9A471296118801 CRC64;
     MTETHRLFLA LLSISLYLLW VAVLLFKQRK ASNLDVSEHA TLVVYASQTG TAEKVARAKA
     AALADMETTS VVSMSDLKLD MLSHVSKAIF VVSTYGEGEP PDAGRKFSSI LKKAYSQSVL
     PLSHLSFEVV GLGDRQYTSF CAFAVSLFDG LNQLGGKAAS PLMTLDSSKG EHLSLLDNLP
     SKNTETSLVL TVNKRTCLNT VNQTLASGGR GLYALSLGIQ KAQTATSWVD DSLWEAGDIL
     EVHIPASQQN TNAEDNVGRE TATRSYTIAS VTSEGDIKLV VRQVVKEDGT LGLGSGLLTH
     SSKLADSISG TIRKNESAYI SDTQCPLILI AAGSGIAGVR AHLAKRASLQ NAGPVWVFYG
     ERHAEFDDVL DITLSPFHQA ACLHKKSTIF SRDENGGYVQ HLLQQHSKQV NAFIGSEGHV
     YVCGDFAGMG KGVDEILKSI LGDGRYEKLH EQGRYHRDLY
//
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