ID F2JUY7_MARM1 Unreviewed; 418 AA.
AC F2JUY7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Biphenyl 2,3-dioxygenase {ECO:0000313|EMBL:ADZ91641.1};
DE EC=1.14.12.18 {ECO:0000313|EMBL:ADZ91641.1};
GN OrderedLocusNames=Marme_2404 {ECO:0000313|EMBL:ADZ91641.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91641.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ91641.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CP002583; ADZ91641.1; -; Genomic_DNA.
DR RefSeq; WP_013661545.1; NZ_CP047696.1.
DR AlphaFoldDB; F2JUY7; -.
DR STRING; 717774.Marme_2404; -.
DR KEGG; mme:Marme_2404; -.
DR PATRIC; fig|717774.3.peg.2486; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
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.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:ADZ91641.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADZ91641.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001062}.
FT DOMAIN 45..164
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 418 AA; 48353 MW; 9A4ED8777CDCDA7F CRC64;
MSQINSNTNE HVWNQEGTCR IPFWTYTNED VHKKELERLF YQKHWCYVGL EAEIPDPGDF
KRTVIGERSV IMVRDQDGSI YVVENLCAHR GMRFCREKQG NTKSFTCPYH QWNYDLEGNL
QGVPFRRGVK QDGQVKGGMP KDFKPADHHL TKLRVAQRGG VVFASFDHDI ESFEDFLGPT
ILSYFDRMFN GRKLTLLGYN KQRIPGNWKL MQENIKDPYH PGLLHTWFVT FGLWRADNRS
ELKMDDHFRH AAMISTRGAG GENAQTTNVS SFKESMTLND PSFLDVEVEP WWDGPTAVMM
TIFPSVILQQ QVNSVSTRHI QPNGHGSFDF VWTHFGYEDD TEEMTERRLR QANLFGPAGF
VSADDGEVIE FSQQGFEQKP NHRSLAELGG KGIEETDHMV SETLIRGMYD YWRKLMEV
//