ID N9MYJ7_9GAMM Unreviewed; 491 AA.
AC N9MYJ7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F903_02595 {ECO:0000313|EMBL:ENW94919.1};
OS Acinetobacter sp. NIPH 298.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217692 {ECO:0000313|EMBL:ENW94919.1, ECO:0000313|Proteomes:UP000018428};
RN [1] {ECO:0000313|EMBL:ENW94919.1, ECO:0000313|Proteomes:UP000018428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 298 {ECO:0000313|EMBL:ENW94919.1,
RC ECO:0000313|Proteomes:UP000018428};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 298.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:ENW94919.1}.
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DR EMBL; APRM01000008; ENW94919.1; -; Genomic_DNA.
DR RefSeq; WP_005197571.1; NZ_KB850055.1.
DR AlphaFoldDB; N9MYJ7; -.
DR STRING; 1217692.F903_02595; -.
DR PATRIC; fig|1217692.3.peg.2558; -.
DR HOGENOM; CLU_001570_17_7_6; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000018428; 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 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 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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..182
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 196..352
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 491 AA; 56705 MW; E33054815543523D CRC64;
MTQPLFLVIC ALLFLLLVHI FIIIYLFWRQ FSQRIDTDIN AQQYLVVYAS QTGQAEAWAK
HTAEQLKIIH EEKVELLDIH ELNYQHLQQP STILWVVSTY GEGDAPDTAQ NFVHKILNQS
LDLAHLSFAV LALGDKRYSN FCQFGQRIEQ WLLQHNAQAL FPTVLVDQLN SDDLEQWLIG
LEQLTSTTFT SIALDKEMLA FKFAHRQCLN TGTVGEAIYK VQLIADRDIS WSSGDILEIQ
CENDITEIQH FLDTQRQEYS DDLVAKLGRL NLRKLPTRTG LSVLEWIAQF EVLPKREYSI
ASLPEQGLVE LVVRQQQTEI GWGLGSGWLT VGLEQNQPVH ASIRNNSSFH LQQDDKPIIL
IGNGTGIAGL VAHLRQREHW GYKKNWLIFG ERQQQFDHLY QTEIAYWQQH GYLPHVDYAF
SRDQTEKIYV QDRLRQQSSR LQEWIAQGAL IYVCGSLKGM ASGVDQVLEE LLGTEQLQQL
KREQRYLRDV Y
//
