ID W5TNY9_9NOCA Unreviewed; 61 AA.
AC W5TNY9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Rubredoxin {ECO:0000256|RuleBase:RU003820};
GN ORFNames=NONO_c63200 {ECO:0000313|EMBL:AHH21090.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH21090.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH21090.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH21090.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
CC -!- FUNCTION: Involved in the hydrocarbon hydroxylating system, which
CC transfers electrons from NADH to rubredoxin reductase and then through
CC rubredoxin to alkane 1 monooxygenase. {ECO:0000256|ARBA:ARBA00002792}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|RuleBase:RU003820};
CC -!- SIMILARITY: Belongs to the rubredoxin family.
CC {ECO:0000256|RuleBase:RU003820}.
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DR EMBL; CP006850; AHH21090.1; -; Genomic_DNA.
DR RefSeq; WP_025352419.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TNY9; -.
DR STRING; 1415166.NONO_c63200; -.
DR KEGG; nno:NONO_c63200; -.
DR PATRIC; fig|1415166.3.peg.6492; -.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_128747_1_1_11; -.
DR OrthoDB; 9800607at2; -.
DR Proteomes; UP000019150; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR PANTHER; PTHR47627; RUBREDOXIN; 1.
DR PANTHER; PTHR47627:SF1; RUBREDOXIN-1-RELATED; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU003820};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003820};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003820};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..56
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 61 AA; 7029 MW; 22317AD53D7311D1 CRC64;
MSGEFRIYQC IQCGFEYDEE QGWPDEGIAP GTRWDDIPDD WTCPDCGAAK ADFFMVEIER
S
//
