ID Q214B9_RHOPB Unreviewed; 1010 AA.
AC Q214B9;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=FAD linked oxidase-like {ECO:0000313|EMBL:ABD88267.1};
GN OrderedLocusNames=RPC_2718 {ECO:0000313|EMBL:ABD88267.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88267.1};
RN [1] {ECO:0000313|EMBL:ABD88267.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88267.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000301; ABD88267.1; -; Genomic_DNA.
DR AlphaFoldDB; Q214B9; -.
DR STRING; 316056.RPC_2718; -.
DR KEGG; rpc:RPC_2718; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_010756_1_0_5; -.
DR OrthoDB; 9811557at2; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 48..280
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 1010 AA; 110206 MW; 0F4EF52500A36E14 CRC64;
MLVRLANSRA PAPRHAELAA ELRARGFEGD LAHAYGERIV AATDNSIYQL LPELVVFPRS
VEDLVRVARV TAEPRFANIV LAPRGGGTGT NGQSLTEGVV VDVSRHMNGI LEINPEERWV
RVQAGVVKDQ LNAALAEHGL FFPPELSTSN RATIGGMIST DASGQGSCLY GKTRDHVLEL
TTVLLDGTAW TSRALEDDEL QQIQQRSDLV GTVHRLIDTV QREQADAIAA HFPKLNRCLT
GYDLAHIRDD RGRFNLNAIL CGSEGTLGLI AEAKLNVVPI PKYSALVNVR YGSFDAALRD
AQDLMRFGAA SIETVDSKVL GLAQDDVVWD SVRQYFPQDD RQRAMGANLV EFVGDSNEKV
EAAIGRIAEA LGSAVPSRGR LGFTVARGAS EVNAIWAMRK KSVGLLGNMH GDKRPIPFVE
DTAVPPENLA DYIAEFRALL DAHGLVYGMF GHVDAGVLHV RPAIDMKDPA QEPLIREITE
QVVQLTEKYG GLLWGEHGKG VRSEFSPRFF GPLYPTLQSI KAAFDPRNQL NPGKIAAPAD
GVLLTIDGLT TRGQIDRVIP APTRAAYDGA LHCNGNGACF TWDPDEAMCP SYKATRDRRH
SPKGRASLTR EWLRQLATLG IDPIAEAAAL RQRSGWRHFP ARLRNSWARE PDFSHAVKEA
MDGCLACKSC SGQCPIKVDV PALRAKFLEI YHGRYLRPLR DHMVGSLETM LPLLGRMGWL
YNAAIASPPG RAALRAIGMV HTPRLSGISM RRELTARGIA MATPQALAAL PVEQRARSVV
LVQDAFTSWH ESHVVLAVLD LMQAIGFRPF IAPLRPNGKP LHVQGFLGAF IRTASSNAAM
LRDLAATGIE LVGVDASMTL TYRSEYDMLA EADRPPPVLL LQEWLARHRD AIPRMVGAGG
EYLLLPHCSE RSLALTSLRD WQTAFAAAGT SLRVLPSGCC GMAGTYGHET EHRASSEQIY
GMSWGRQVKR WAQSGRLLAT GYSCRSQVKI IDGQMLAHPA QALLACLGKR
//