ID U2ZGS3_VIBPR Unreviewed; 606 AA.
AC U2ZGS3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Flavodoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=VPR01S_05_01610 {ECO:0000313|EMBL:GAD66866.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD66866.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD66866.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD66866.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:GAD66866.1}.
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DR EMBL; BATJ01000005; GAD66866.1; -; Genomic_DNA.
DR RefSeq; WP_021704844.1; NZ_BATJ01000005.1.
DR AlphaFoldDB; U2ZGS3; -.
DR STRING; 1219065.VPR01S_05_01610; -.
DR eggNOG; COG1018; Bacteria.
DR eggNOG; COG3217; Bacteria.
DR Proteomes; UP000016570; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06215; FNR_iron_sulfur_binding_1; 1.
DR Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022692};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000016570};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 115..265
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 278..381
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 522..606
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 606 AA; 66971 MW; 3849BC1BCCF90E5D CRC64;
MSSSSRLTQI NVYPVKSVAG IAISSAWVEK QGLAFDRRFM VATSDGVMVT ARKYPHMVKV
QSSLTADGII FTAPDQPALK LRYADFKHQA APATVWNDSF EAYTTTDEAD DWFSDALGQR
VELLYTGEQS NRVPERVGNN VSFADGFPVL VISEGSLDEL NRRSSESHLM DQFRTNLVVS
GGEPFVEDSW KRIRIGEVEF ESVKPCSRCI LTTVDIDKGA FKPSKEPLKT LSQFRANRSG
DVFFGQNLIA LNEGMIHAGD PVEVLEYKEK EQYEDHSPSR MTLTCVQREE IARDFVTFWL
EPDSESLPTY LPGQHLPIEV AIGGERIGRR YTLSSSPSRP GRLAISVKRI DAGRVSNWLL
DNLQVGDTLE AESPSGSFHL GEKHDQPILL LSAGSGVTPM LSMLRYLADH DQVRDVVFYH
QCRTESDIPC KQELEGLERQ HPGLKVVLSL TQPAPDWFGL KGRLTLSHLK QIKDVEQRQV
FVCGPDGFMQ KAKNLLLKQG LPESMYHQEA FGVAISAPKA LKTLQISVNG TLFEGNNQAT
LLEQAEAAGV PISNSCRAGL CGACRVTVES GKVDQPDVPA LQDNDRHMGI ALACCCVPET
DIEVVN
//
