ID   K1U257_9ZZZZ            Unreviewed;       130 AA.
AC   K1U257;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   SubName: Full=Desulfoferrodoxin {ECO:0000313|EMBL:EKC76363.1};
DE            EC=1.15.1.- {ECO:0000313|EMBL:EKC76363.1};
GN   ORFNames=OBE_00883 {ECO:0000313|EMBL:EKC76363.1};
OS   human gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC76363.1};
RN   [1] {ECO:0000313|EMBL:EKC76363.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA   Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA   Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA   Suarez A.;
RT   "Microbiota from the distal guts of lean and obese adolescents exhibit
RT   partial functional redundancy besides clear differences in community
RT   structure.";
RL   Environ. Microbiol. 15:211-226(2013).
CC   -!- SIMILARITY: Belongs to the desulfoferrodoxin family.
CC       {ECO:0000256|ARBA:ARBA00005941}.
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:EKC76363.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJWZ01000598; EKC76363.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1U257; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.28.100; Desulphoferrodoxin, N-terminal domain; 1.
DR   Gene3D; 2.60.40.730; SOR catalytic domain; 1.
DR   InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR   InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR   InterPro; IPR004462; Desulfoferrodoxin_N.
DR   InterPro; IPR038094; Desulfoferrodoxin_N_sf.
DR   NCBIfam; TIGR00332; neela_ferrous; 1.
DR   PANTHER; PTHR36541; SUPEROXIDE REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR36541:SF1; SUPEROXIDE REDUCTASE-RELATED; 1.
DR   Pfam; PF06397; Desulfoferrod_N; 1.
DR   Pfam; PF01880; Desulfoferrodox; 1.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   SUPFAM; SSF49367; Superoxide reductase-like; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:EKC76363.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          11..40
FT                   /note="Desulfoferrodoxin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06397"
FT   DOMAIN          47..129
FT                   /note="Desulfoferrodoxin ferrous iron-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01880"
SQ   SEQUENCE   130 AA;  14691 MW;  43A9E9BBEB53F840 CRC64;
     MEGEKGMEVR YYICKHCGNI VEKVKDKGVP VICCGEPMQE LKAGVTDAAV EKHVPVYTIE
     GSHVHVVVGE TKHPMLEEHF IEWITLNTNQ GIYRKQLNPG QEPVADFCLC DGEQVEEVYA
     YCNLHGLWKC
//