ID A1TGX2_MYCVP Unreviewed; 520 AA.
AC A1TGX2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Rieske (2Fe-2S) domain protein {ECO:0000313|EMBL:ABM16422.1};
GN OrderedLocusNames=Mvan_5657 {ECO:0000313|EMBL:ABM16422.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16422.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM16422.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
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., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR EMBL; CP000511; ABM16422.1; -; Genomic_DNA.
DR RefSeq; WP_011782774.1; NZ_JACKSD010000095.1.
DR AlphaFoldDB; A1TGX2; -.
DR STRING; 350058.Mvan_5657; -.
DR KEGG; mva:Mvan_5657; -.
DR eggNOG; COG2146; Bacteria.
DR eggNOG; COG2220; Bacteria.
DR HOGENOM; CLU_525630_0_0_11; -.
DR Proteomes; UP000009159; Chromosome.
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 Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR15032; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR15032:SF4; N-ACYL-PHOSPHATIDYLETHANOLAMINE-HYDROLYZING PHOSPHOLIPASE D; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 4: Predicted;
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:UP000009159}.
FT DOMAIN 469..520
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 520 AA; 58499 MW; C877EF51126FCBAA CRC64;
MQVTSVGHAG FRIDTKAGSI LCDPWLNPAY FASWFPFPDN SDLDWAALGD VDYLYVSHLH
KDHFDPQNLR DHVNKDAVVL LPDFPVPDLR RELEKLGFHR FFETADSVKH RVSGPKGELD
VMIVALRAPA DGPIGDSGLV VDDGETTVFN MNDARPVDLD MLHTDFGQID VHMLQYSGAI
WYPMVYDMPA RAKEAFGIQK RQRQMDRCRQ YIAQVGATWV IPSAGPPCFL DPELRGLNDD
HGDPANIFPD QVVFLDQMRT HGHDGGLLMI PGSAADFAGS QLRSLTHPIP DDDVQAIFTT
GKADYIADYA ERMAPVLAAE RASWAPAAGK PLLEPLRELF EPIMLASDQI CDGIGYPVEL
RLHSRGHEET IVLDFPKRAV REAIPDEKFR YGFAIAPELV RTVVRDREPD WVNTIFLSTR
FTAWRVGGYN EYLYTFFKCL TDERIAYADG WFAEAHDDCA SITLDGWEIQ RRCPHLKADL
SKFGVVEGNT LTCNLHGWQW NLTNGRCLTT NGHELRSAKL
//
