ID A0A368TU83_9GAMM Unreviewed; 318 AA.
AC A0A368TU83;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:RCV88315.1};
GN ORFNames=DU506_14915 {ECO:0000313|EMBL:RCV88315.1};
OS Halomonas rituensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2282306 {ECO:0000313|EMBL:RCV88315.1, ECO:0000313|Proteomes:UP000253204};
RN [1] {ECO:0000313|EMBL:RCV88315.1, ECO:0000313|Proteomes:UP000253204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TQ8S {ECO:0000313|EMBL:RCV88315.1,
RC ECO:0000313|Proteomes:UP000253204};
RA Lu H., Xing P., Wu Q.;
RT "Halomonas rutogse sp. nov., isolated from Lake TangqianCo on Tibetan
RT Plateau.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RCV88315.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QPIJ01000040; RCV88315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368TU83; -.
DR OrthoDB; 4258484at2; -.
DR Proteomes; UP000253204; 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; cd06185; PDR_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; 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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
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..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..318
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 318 AA; 34603 MW; 826A33A0A6D1E791 CRC64;
MQDDIITLRV VRRDAHTNEI AVIDLAAVDG GELPAFEAGS HIDIHLDDGM IRQYSLSNPP
GERHRYRLGV LLDPASRGGS QAVHERLHEG TEVKVSVPRN LFPLDESAPH SLLLGGGIGI
TPMIAMAYAL QAEGRSFELH YCCRSREKAA FIDELESTFG DALVLHFDDG EPSQHLHIET
VLAAQPADTH LYVCGPTGFM DWVIGVTQKV DWPKPRVHSE YFTAEVDTSG AAFEVEAVAS
GVTVQVEEGM SIAQALKAAG VKVNVSCEEG VCGTCISEVL EGVPDHRDHF LSDEEKEDND
QIAVCCSRAK TPRLVIDI
//