ID A0A0H2LTR9_VARPD Unreviewed; 335 AA.
AC A0A0H2LTR9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase {ECO:0000313|EMBL:KLN53599.1};
DE EC=1.17.1.- {ECO:0000313|EMBL:KLN53599.1};
GN Name=ascD3 {ECO:0000313|EMBL:KLN53599.1};
GN ORFNames=VPARA_52850 {ECO:0000313|EMBL:KLN53599.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN53599.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN53599.1, ECO:0000313|Proteomes:UP000035170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN53599.1,
RC ECO:0000313|Proteomes:UP000035170};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KLN53599.1}.
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DR EMBL; JZWI01000032; KLN53599.1; -; Genomic_DNA.
DR RefSeq; WP_047786630.1; NZ_JZWI01000032.1.
DR AlphaFoldDB; A0A0H2LTR9; -.
DR PATRIC; fig|34073.19.peg.5402; -.
DR Proteomes; UP000035170; Unassembled WGS sequence.
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:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06189; flavin_oxioreductase; 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; 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 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};
KW Oxidoreductase {ECO:0000313|EMBL:KLN53599.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170}.
FT DOMAIN 3..92
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 98..197
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 335 AA; 36838 MW; 5328A07EDE5DE349 CRC64;
MAYRIQLLET AQTFIAQAGE SVLEAALRQD QRLPHECRFG GCGTCRIRLV EGAVRYDEFP
PGLTPEEAAE GYALACQAQP ESDLVISAAR HLPPCSEPAR HVATVKAVRP LAEDVLHLAL
EVPCEAELLY RAGQYINILL PDGSHRSFSM ASRPHPQVLD FHIRRIPEGR FTSGDAARLQ
PGDRLPVELP HGTFCYHAED YRPLIMVATG TGLAPIKSIL ESLMDDEDCP PVSLYWGMRT
EADLYLHDEI QAWAGRLCDF RYVPVLSRAG AGWNGRRGHV QDAVLADVDD LSEHAIYLCG
SPAMIGDAKR AFLARGASID QLYSDSFTFQ SAIAA
//
