ID A0A2S9KAV9_9BURK Unreviewed; 325 AA.
AC A0A2S9KAV9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PRD67522.1};
GN ORFNames=C6P61_15890 {ECO:0000313|EMBL:PRD67522.1};
OS Malikia spinosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Malikia.
OX NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD67522.1, ECO:0000313|Proteomes:UP000238326};
RN [1] {ECO:0000313|EMBL:PRD67522.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=83 {ECO:0000313|EMBL:PRD67522.1};
RA Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT serpentinized springs.";
RL Submitted (MAR-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:PRD67522.1}.
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DR EMBL; PVLR01000056; PRD67522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9KAV9; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000238326; 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 1..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 240..325
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 325 AA; 34589 MW; 13B3AC743C873417 CRC64;
MTASPLLQVR VRALTYEAQG ILGIELVPLS AENPLPAFSA GSHIDLHLPT PQGPLIRSYS
LLNDPRETHR YCIGVNKDAR SRGGSAYVHA SLRAGDILTI SAPRNNFPLD EAAPHQVFIA
GGIGITPMLG MLARAQALGT PWTLYYTART RAHAGFLDLL ETAAGAGNGQ VVLNFDQEPG
GRMLDLPAIV AALPAGAHLY CCGPLPMLEA YEKATAGLPA ARVHKEYFAA KDAPATEGGF
TVELVRSRQS LQVPAGKSIL DCLIEICAEP PYSCREGICG TCEVKVLEGT PDHRDLVLSD
SERAANDRML VCCSGARSAR LVLDL
//