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Database: UniProt
Entry: A0LGG5_SYNFM
LinkDB: A0LGG5_SYNFM
Original site: A0LGG5_SYNFM 
ID   A0LGG5_SYNFM            Unreviewed;       192 AA.
AC   A0LGG5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Putative heterodisulfide reductase, C subunit {ECO:0000313|EMBL:ABK16517.1};
GN   OrderedLocusNames=Sfum_0820 {ECO:0000313|EMBL:ABK16517.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16517.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16517.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HdrC family.
CC       {ECO:0000256|ARBA:ARBA00007097}.
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DR   EMBL; CP000478; ABK16517.1; -; Genomic_DNA.
DR   RefSeq; WP_011697690.1; NC_008554.1.
DR   AlphaFoldDB; A0LGG5; -.
DR   STRING; 335543.Sfum_0820; -.
DR   KEGG; sfu:Sfum_0820; -.
DR   eggNOG; COG1150; Bacteria.
DR   HOGENOM; CLU_093432_1_0_7; -.
DR   InParanoid; A0LGG5; -.
DR   OrthoDB; 9769677at2; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43255:SF1; FERREDOXIN_F(420)H(2)-DEPENDENT COB-COM HETERODISULFIDE REDUCTASE SUBUNIT C; 1.
DR   PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN          21..52
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   192 AA;  21531 MW;  FC799538D3DC3D33 CRC64;
     MNEQSSGATT AHGGSAAAGP LDPIAEKVSA CMQCGTCTGS CANAFAMDYT PRQLWRLVQL
     GEQDEIFRST TFWMCSSCYY CTLRCPRGLP LTETIQALKR IAFARGTYRS KTSPVFYSTF
     VDNIRRYGRV REMDMMTRFF LRLKHPVAPL RFASLGVKLL RKGKISPQMP ALFAKGKLDG
     LFRKVRELES ES
//
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