ID A0A0P0NZ40_9CAUL Unreviewed; 654 AA.
AC A0A0P0NZ40;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=FAD-binding oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQ619_07075 {ECO:0000313|EMBL:ALL13131.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL13131.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL13131.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL13131.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013002; ALL13131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0NZ40; -.
DR STRING; 69395.AQ619_07075; -.
DR KEGG; chq:AQ619_07075; -.
DR OrthoDB; 9786134at2; -.
DR Proteomes; UP000056905; Chromosome.
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; cd06184; flavohem_like_fad_nad_binding; 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; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR42815; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR PANTHER; PTHR42815:SF2; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01243; Putative_PNPOx; 2.
DR PRINTS; PR00406; CYTB5RDTASE.
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:UP000056905}.
FT DOMAIN 292..392
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 565..654
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 654 AA; 70390 MW; 7800374B04B802F3 CRC64;
MPDQHRTFFE QLPIVVLGSR DVSGQPWATL LDGTPGFIKS PSPVELTIAA TFSHGDPAAE
GVATGQPVGL LGIELHTRRR NRMNGRISAR GPEGFSIAVD QSFGNCPQYI QGRNFEHVDQ
ALISQRAAPE RTAGLSREAA SLVASADTFF IASAHTDKAA QDPVHGVDVS HRGGKPGFVR
VQGDVLTIPD FLGNFLFNTL GNILVEPRVG LVFPDFSNGD LWHLSATAKI IWEGPEVDGF
AGAERLLQFT VVETVKVAAS LSIRAVGEVE PSPYLDKTGS WEAVDASGWG KKEFRPFRVA
WAEPETETVR SVVLKPLDGG SVPVHRAGQH IFVRLNVNGS QDLRPYTVSD AANGSSYRIS
VKRQGRFSEA VHQLKIGDVV ELLPPRGDFV FDEAAPRPAV LLSAGIGVTP MIAMINRILV
NNGRSRSQQR LWFFHGARNS LDHAFRHHMI DKSSRHSNLT IVTAYNEPLP GDVLGRDYDV
NGWVNLDLLK AKLPFDDYEF YLCGPPPFMD ALSKGLLGMG VRPERIHSEA FGPAAIKPAA
VGASLGSKAT PPSSGAAAKA DGHAAEVEFQ ASGKRATWRS GEGTLLELAE REGLKPIHSC
RSGTCGVCAV KLIQGSVDYV NNPTAPCEDD EVLICSAVPS RSDDDASVSI VLDV
//
