ID N8ZSY9_9GAMM Unreviewed; 908 AA.
AC N8ZSY9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=F960_00833 {ECO:0000313|EMBL:ENV34868.1};
OS Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV34868.1, ECO:0000313|Proteomes:UP000013117};
RN [1] {ECO:0000313|EMBL:ENV34868.1, ECO:0000313|Proteomes:UP000013117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV34868.1,
RC ECO:0000313|Proteomes:UP000013117};
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 gerneri CIP 107464.";
RL Submitted (FEB-2013) 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:ENV34868.1}.
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DR EMBL; APPN01000051; ENV34868.1; -; Genomic_DNA.
DR RefSeq; WP_004857211.1; NZ_KB849537.1.
DR AlphaFoldDB; N8ZSY9; -.
DR STRING; 202952.GCA_000747725_00284; -.
DR GeneID; 84208247; -.
DR PATRIC; fig|1120926.3.peg.797; -.
DR eggNOG; COG0369; Bacteria.
DR eggNOG; COG3182; Bacteria.
DR HOGENOM; CLU_001570_17_4_6; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000013117; 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; 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; IPR005625; PepSY-ass_TM.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR34219:SF3; BLL7967 PROTEIN; 1.
DR PANTHER; PTHR34219; IRON-REGULATED INNER MEMBRANE PROTEIN-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03929; PepSY_TM; 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 Reference proteome {ECO:0000313|Proteomes:UP000013117};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 455..593
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 228..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 102483 MW; 8B7A4274E050E3F6 CRC64;
MLKKFFFQIH WFLGITAGLI LSIMGLTGAI FSYEQPIQKW INPSSFTVEV PNHQNKLSPA
EIFQHFQKNT PDIKINSITI DQDPSASSSI NIVKEGARRG YTMMINPYTA EVLPEVKGRE
FFAFIQQLHR NLTAGEVGKQ ITGACTLMLL FFIFSGLYLR WPKKHTWRQW FVIKPKLKGR
NFLWDLHAVV GTWVIVFYLL LACTGLFWSY DWWRNGMYKV MGVERPAPQM QGEGGKGPRD
GENARGPRDG ENARGPRDGA DANPENRQGD RANLQGNENR SARSEQGRQS EQANDQRDQK
EGKKGLSPEQ VNLALTQTWT AIQNNLGHGY SSISLNIPKK PDGKLEITFV DPVVQHERAR
NKVSFDYQNA QFGKFDLYED KKLNEKIMSS MLPVHRGSFF GPVYQFLVML ASLMMPLFFV
TGWMLYLKRR KQKKLTLAAR NLAPMGTLDL NATPWLIVYA SQTGVAEQLA WRTASSLREA
SLPKSVIAIQ KLTSNDLKNA LHIIFIASTY GTGEAPDLAT SFSKKLMHEK LDLSHLSFAV
LALGSKEYPE SYCQFGHGIA AWLKENAAQA LFPTVEVDNG NPADLQKWNT ALAAATQLDL
QEVVIEKAFS EWSLQQRDLL NPDSLGAPAF HIQLKTTQEL TWQAGDIAEI QTANSINRVR
KFLEKYHIDA NTQLSTTGQT IAQALHEKDL SQELDFNDLD DLVAKLPLLP TREYSIASIP
SQQVLALVIR QTIDENGELG LGSGFMTQHL ALYDKVNVNI RTNEAFHLIE GPRPIICIGN
GTGIAGLMSL LNARIEDGQA ENWLIFGERQ SERDYFFKDT IQSWQETGKL KRLDLAFSRD
QEHKVYVHHK LRENADMLKQ WLENGAAIYV CGSIQGMAGG VEQALIDILG VEKLDELREA
KRYRRDVY
//
