ID Q84IA2_9PSED Unreviewed; 336 AA.
AC Q84IA2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=B1,2O reductase component {ECO:0000313|EMBL:AAO19115.1};
GN Name=XylZ {ECO:0000313|EMBL:AAO19115.1};
OS Pseudomonas sp. S-47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=115714 {ECO:0000313|EMBL:AAO19115.1};
RN [1] {ECO:0000313|EMBL:AAO19115.1}
RP NUCLEOTIDE SEQUENCE.
RA Park D.-W., Kim Y., Lee S.-M., Ka J.-O., Kim C.-K.;
RT "Cloning and Sequence Analysis of the xylL Gene Responsible for 4CBA-
RT Dihydrodiol Dehydrogenase from Pseudomonas sp. S-47.";
RL J. Microbiol. 38:275-280(2000).
RN [2] {ECO:0000313|EMBL:AAO19115.1}
RP NUCLEOTIDE SEQUENCE.
RA Park D.-W., Kim C.-K.;
RT "Analysis of xyl operon responsible for 4-chlorobenzoate degradation from
RT Pseudomonas sp. S-47.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR EMBL; AF320981; AAO19115.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84IA2; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06209; BenDO_FAD_NAD; 1.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR047683; BenC-like_FAD_NAD-bd.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; NF040810; BenC; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 3..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 104..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 336 AA; 36212 MW; C044D828766A57A2 CRC64;
MTHKVALNFE DGVTRFIDAN AGETVADAAY RQGINLPLDC RDGACGACKC FAESGRYSLG
EEYIEDALSE AEAEQGYVLT CQMRAESDCV IRVPAASDVC KTQQASYQAA ISNVRQLSES
TIALSIKSAS LNQLAFLPGQ YVNLQVPGSD QTRAYSFSSL QKDGEVGFLI RNVPGGLMSS
FLTSLAKVGD SVSLAGPLGA FYLREIKRPL LLLAGGTGLA PFTAMLEKIA EQGSEHPLHL
IYGVTHDHDL VEMDKLEAFA ARIPNFSYTA CVASPDSAYP QKGYVTQYIE PKHLNGGEVD
VYLCGPPPMV EAVSQYIRAQ GIQPANFYYE KFAASA
//
