ID A0A1E4J8L4_9BURK Unreviewed; 455 AA.
AC A0A1E4J8L4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Hydrogenase {ECO:0000313|EMBL:ODU18974.1};
GN ORFNames=ABS94_01895 {ECO:0000313|EMBL:ODU18974.1};
OS Variovorax sp. SCN 67-85.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU18974.1, ECO:0000313|Proteomes:UP000094461};
RN [1] {ECO:0000313|EMBL:ODU18974.1, ECO:0000313|Proteomes:UP000094461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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:ODU18974.1}.
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DR EMBL; MEFM01000003; ODU18974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4J8L4; -.
DR Proteomes; UP000094461; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; 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 Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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}.
FT DOMAIN 44..142
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 455 AA; 52258 MW; 28EA57DFE37F3F11 CRC64;
MIPITTESRY NAMINLRKGE ISREIFSSKD IFEEELERVF TRAWLFVGHE SQIPNPGDFF
TSRMGAESVI LARDKKKQVH VFLNSCRHRG MKVCQYDHGN TQLFTCPYHS WSYTTEGKLF
GVPQFKNLYE GCLEKDDWSL IEVPKMQTYK GTVWASWDKD APDLLTYLGD AKTHLDLALD
CRDGREGGSE VLVGVHKWII PCNWKFAAEN FLGDTYHNVS HRSVDMIGIG PSAEAGAKGR
RDNELEKAQH VWVNFPAGHG VHSAIMPSTW EFLDTYQNNP IVAEYFREAH ARRKERLGAE
RHRLVPFVGT IYPNVSFHGN QPRNLCVWHP HGPESTEAWR FFLVDADAPQ EVKDFLRTYY
MRYSGPAGMT EQDDMENWNY ATAGSRGVIA KRYPYNYQQS LGKVQTTGPV AGNVSLQVSE
ENPRQFYRRW RDYMNAADWD TLLGRNDKEP ASFAG
//
