ID A1TDE1_MYCVP Unreviewed; 446 AA.
AC A1TDE1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Phenylpropionate dioxygenase alpha subunit {ECO:0000313|EMBL:ABM15191.1};
DE EC=1.14.12.19 {ECO:0000313|EMBL:ABM15191.1};
GN OrderedLocusNames=Mvan_4415 {ECO:0000313|EMBL:ABM15191.1};
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:ABM15191.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM15191.1, 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};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP000511; ABM15191.1; -; Genomic_DNA.
DR RefSeq; WP_011781569.1; NZ_JACKSD010000061.1.
DR AlphaFoldDB; A1TDE1; -.
DR STRING; 350058.Mvan_4415; -.
DR KEGG; mva:Mvan_4415; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_11; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000313|EMBL:ABM15191.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABM15191.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 38..121
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 446 AA; 50802 MW; E7ADB3C5CDB15120 CRC64;
MIDFTDLVDP EHGWVSPQIY TDPEIYEREL QHVFGRSWLF LAHDSQLPKP GSFLQTYMGE
DPVLVVRQRD GSVRAFLNQC RHRGMRICRS EAGVSKAFTC TYHGWSYDLA GNLINVPLEE
RAYHSSIDKK EWGAMKVPRV ANYRGFYFGT WSEETPEFDA YLGDMAFYFD AIVDRFDSGL
EFVKGTTKWV IDCNWKFASE QFASDMYHTQ SAHASALLAL TDDPNPIGPL NDPNVPGRQF
SGNGHGSGGY FLPAPVVKTP EMTDTMFEWF KSREEEMVAR IGADRLSKVS ITHNTIFPNF
SWLGAHSTMR VWHPRGPGQI EVWAWTYVPK DAPPKVKNEI RELTQRTFSP AGSFETDDGE
NWTEIQQVLR GSQARRNRLH TAMGVGYEER DAFGLPGLGN DVYSETAARG FYRHWLDMLT
GKPWSEIQKW TPNGNHGELR DEGVTA
//