ID A0A238D5N8_THIDL Unreviewed; 344 AA.
AC A0A238D5N8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase {ECO:0000313|EMBL:SBP88627.1};
DE EC=1.17.1.- {ECO:0000313|EMBL:SBP88627.1};
GN Name=ascD {ECO:0000313|EMBL:SBP88627.1};
GN ORFNames=THIARS_70247 {ECO:0000313|EMBL:SBP88627.1};
OS Thiomonas delicata (Thiomonas cuprina).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=364030 {ECO:0000313|EMBL:SBP88627.1, ECO:0000313|Proteomes:UP000214566};
RN [1] {ECO:0000313|EMBL:SBP88627.1, ECO:0000313|Proteomes:UP000214566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16361 {ECO:0000313|EMBL:SBP88627.1,
RC ECO:0000313|Proteomes:UP000214566};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FLMQ01000056; SBP88627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238D5N8; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000214566; 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:SBP88627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214566}.
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..200
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 344 AA; 37763 MW; 819EFBDDAB479F53 CRC64;
MSFEVKVLPS NHRFDVGDGE TVLAAAIRQG VGLPYGCQDG ACGSCKCRWV AGEFELGIHQ
LKALGEAERA AGFILACRTK PTSDLVIESH ELPAEGMYPV KKMPCRVMTI ERPASDVAVI
RLQLPANDDF AYHAGQYVQF ILRDGSRRSY SMANAPRGER QIELHLRHMP GGKFTDHVFG
AMKEKDILRM EGPFGSFYLR EDSDKPMVLL ASGTGLAPIK AIIEAMRDKD LQRPAVLYWG
CRGKSDLYLH AWAEEQAAAL PWLRYVPVLS EPRPEDAWSG RTGFVHRAVM ADLPDLSGHE
VYACGAPVMV ESARADFVAQ CGLPEDAFYA DAFTSEADKT GPAG
//
