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Database: UniProt
Entry: C5AVS6_METEA
LinkDB: C5AVS6_METEA
Original site: C5AVS6_METEA 
ID   C5AVS6_METEA            Unreviewed;       165 AA.
AC   C5AVS6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Oxidoreductase, 2Fe-2S subunit {ECO:0000313|EMBL:ACS40762.1};
GN   OrderedLocusNames=MexAM1_META1p3014 {ECO:0000313|EMBL:ACS40762.1};
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS40762.1, ECO:0000313|Proteomes:UP000009081};
RN   [1] {ECO:0000313|EMBL:ACS40762.1, ECO:0000313|Proteomes:UP000009081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC   {ECO:0000313|Proteomes:UP000009081};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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DR   EMBL; CP001510; ACS40762.1; -; Genomic_DNA.
DR   RefSeq; WP_003597405.1; NC_012808.1.
DR   AlphaFoldDB; C5AVS6; -.
DR   STRING; 272630.MexAM1_META1p3014; -.
DR   KEGG; mea:Mex_1p3014; -.
DR   eggNOG; COG2080; Bacteria.
DR   HOGENOM; CLU_052511_3_1_5; -.
DR   OrthoDB; 9792018at2; -.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
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   PANTHER; PTHR45331:SF2; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR45331; OXIDOREDUCTASE, IRON-SULPHUR BINDING SUBUNIT-RELATED-RELATED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT   DOMAIN          3..80
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   165 AA;  17362 MW;  FB3FFBE77A3E6568 CRC64;
     MTFRLTLTVN GEPRAIELDD PRVTLLDLLR ERLGLTGSKK GCDRGQCGAC TVLLNGRRIN
     SCLALAVSLD GAEVLTIEGL AVGEQLHPVQ AAFIEHDGFQ CGFCTPGQIM SAVGLIHEGH
     AGDDPERVRE GMSGNLCRCG AYIGITEAVL DAQARSAGVD QGEAA
//
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