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Database: UniProt
Entry: M7NXJ3_9GAMM
LinkDB: M7NXJ3_9GAMM
Original site: M7NXJ3_9GAMM 
ID   M7NXJ3_9GAMM            Unreviewed;       317 AA.
AC   M7NXJ3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Ferredoxin {ECO:0000313|EMBL:EMR13508.1};
GN   ORFNames=MPL1_04682 {ECO:0000313|EMBL:EMR13508.1};
OS   Methylophaga lonarensis MPL.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13508.1, ECO:0000313|Proteomes:UP000012019};
RN   [1] {ECO:0000313|EMBL:EMR13508.1, ECO:0000313|Proteomes:UP000012019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPL {ECO:0000313|EMBL:EMR13508.1,
RC   ECO:0000313|Proteomes:UP000012019};
RX   PubMed=23661481;
RA   Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA   Murrell J.C., Shouche Y.S.;
RT   "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT   (Non-Methane-Utilizing) Methylotroph.";
RL   Genome Announc. 1:E00202-13(2013).
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:EMR13508.1}.
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DR   EMBL; APHR01000021; EMR13508.1; -; Genomic_DNA.
DR   RefSeq; WP_009725952.1; NZ_APHR01000021.1.
DR   AlphaFoldDB; M7NXJ3; -.
DR   STRING; 1286106.MPL1_04682; -.
DR   PATRIC; fig|1286106.3.peg.941; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000012019; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06185; PDR_like; 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; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012019}.
FT   DOMAIN          1..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          230..317
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   317 AA;  34962 MW;  E342D254D74617A4 CRC64;
     MTTLNVRVAA VEQVTELVKH FTLVQQNGQP LPRFSGGSHV VVSMNINGRN HRNPYSLMGS
     PDNTESYHIS VRRQEQSRGG SVYMHDQVTV GSELQITYPV NLFAISKLAH KHILVAGGIG
     ITPFMSQIAD LNRLGQHYEL HYAYRSPEHG AFVEQLREMC GDRLHCYVES EGQRMSFQQL
     LSQQPLGTHV YTCGPDAMVK TLLLTARDMG WPESHLHSEQ FSAPPIGDAF VISLAQSGID
     LEVPGDMSML EAMEEAGLEP PFLCRGGACG RCELEVLACD GALMHNDHYL SDAEKTAGNK
     IMPCVSRASC QKLVLNI
//
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