ID A0A0Q8Q2Z8_9ACTN Unreviewed; 112 AA.
AC A0A0Q8Q2Z8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:KRB76078.1};
GN ORFNames=ASE01_13680 {ECO:0000313|EMBL:KRB76078.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB76078.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB76078.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76078.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB76078.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76078.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000256|ARBA:ARBA00038001}.
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:KRB76078.1}.
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DR EMBL; LMIA01000010; KRB76078.1; -; Genomic_DNA.
DR RefSeq; WP_056753406.1; NZ_LMIA01000010.1.
DR AlphaFoldDB; A0A0Q8Q2Z8; -.
DR STRING; 1736488.ASE01_13680; -.
DR OrthoDB; 147178at2; -.
DR Proteomes; UP000050886; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProt.
DR CDD; cd03528; Rieske_RO_ferredoxin; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR21496; FERREDOXIN-RELATED; 1.
DR PANTHER; PTHR21496:SF0; RIESKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 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:UP000050886}.
FT DOMAIN 10..110
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 112 AA; 11964 MW; 6511F26F21288F5D CRC64;
MESAQMVERR FACNEGDLAP GESMTVPVEG PGTVAVAVYL TEEGAYFATA DTCTHEDWSL
GEDSDLEGNE IVCPLHMARF DIRSGEALCF PATIALATFE VVVDAGKVYV LG
//
