ID A0A133XJK2_9RHOO Unreviewed; 338 AA.
AC A0A133XJK2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:KXB31107.1};
GN ORFNames=AT959_10465 {ECO:0000313|EMBL:KXB31107.1};
OS Dechloromonas denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB31107.1, ECO:0000313|Proteomes:UP000070186};
RN [1] {ECO:0000313|EMBL:KXB31107.1, ECO:0000313|Proteomes:UP000070186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB31107.1,
RC ECO:0000313|Proteomes:UP000070186};
RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT versus atypical NosZ.";
RL Submitted (DEC-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:KXB31107.1}.
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DR EMBL; LODL01000019; KXB31107.1; -; Genomic_DNA.
DR RefSeq; WP_066882912.1; NZ_LODL01000019.1.
DR AlphaFoldDB; A0A133XJK2; -.
DR STRING; 281362.AT959_10465; -.
DR Proteomes; UP000070186; 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:InterPro.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000070186}.
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 338 AA; 37009 MW; F7B7E6711DB32F57 CRC64;
MSHQITVQPS GRQFAAESDE TILDAALRHG LTMPYGCKDG ACGACKGKVL SGSIDHGKAQ
PHALKDDEKA AGMALFCCAR AESDLTLECR QLASASDIPV KTLPSRIEKL EKLAPDVIEM
HLRLPASERL QFLAGQYIDI LLKDGKKRSF SLANAPHDDA VLQLHIRYVP GGLFTEQVFN
SIKVRDILRF NGPHGSFYLR EESTKPMIML AGGTGFAPLK AIVEHAIAEE CTRPIHIYWG
AKARVDLYQN ALPEQWAAAH PNIRYIPVLS EPAVDDAWPG RTGLVHQAVM ADFPDLSGHQ
VYACGAPVMI DAAKRDFTAR CGLPEEEFFA DAFTFSTN
//
