ID A0A162DKM9_9FLAO Unreviewed; 346 AA.
AC A0A162DKM9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Nitric oxide dioxygenase {ECO:0000313|EMBL:KZS41858.1};
GN ORFNames=AWE51_20165 {ECO:0000313|EMBL:KZS41858.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS41858.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS41858.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS41858.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) 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:KZS41858.1}.
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DR EMBL; LQRT01000003; KZS41858.1; -; Genomic_DNA.
DR RefSeq; WP_066311293.1; NZ_LQRT01000003.1.
DR AlphaFoldDB; A0A162DKM9; -.
DR STRING; 1642818.AWE51_20165; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000076715; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 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:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00371; FPNCR.
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 Dioxygenase {ECO:0000313|EMBL:KZS41858.1};
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:KZS41858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076715}.
FT DOMAIN 1..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 256..346
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 346 AA; 39128 MW; DD676B1FFE48C389 CRC64;
MLLTVKDIIP ETKDTVSVIL KNNLFFNKIR YKAGQFLTVK IPIKNKIEKR AYSFSSSPVT
DNFLKITVKK VEKGLVSSYI CDTLKPGQKI EIEKPAGSFY VVPNKNTQFN YILFAAGSGI
TPIFSIIKTV LEKEPLSKII LIYANRNEES TIFKKAIENL EEKYPNSFAV EHILEKKSSK
KPNYHQDLLN KELVDNILKK HHATYEKGNY MMCGPHGFMD KAKEILLERG ITRDKIKLEA
FNTNLITSSD AKKLESAVTI YHDNKKHILD IKGDKTILQA AMANNIMLPY SCRSGMCSSC
KAKCISGTVK MIDGHFLSEE EVEEGHILTC ISFPRSNNVS ISFIND
//
