ID J0WC96_RHILT Unreviewed; 478 AA.
AC J0WC96;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EJC82823.1};
GN ORFNames=Rleg4DRAFT_4552 {ECO:0000313|EMBL:EJC82823.1};
OS Rhizobium leguminosarum bv. trifolii WSM2297.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=754762 {ECO:0000313|EMBL:EJC82823.1, ECO:0000313|Proteomes:UP000005732};
RN [1] {ECO:0000313|EMBL:EJC82823.1, ECO:0000313|Proteomes:UP000005732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2297 {ECO:0000313|EMBL:EJC82823.1,
RC ECO:0000313|Proteomes:UP000005732};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R.,
RA O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft Sequence of Rhizobium leguminosarum bv.
RT trifolii WSM2297.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; JH719395; EJC82823.1; -; Genomic_DNA.
DR AlphaFoldDB; J0WC96; -.
DR HOGENOM; CLU_017779_4_1_5; -.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000005732; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 41..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 50787 MW; 1D41A47135477439 CRC64;
MSSTGISTEL LDRFAAIVGD KYALRAEADL APHLIENRGL YHGSSPLLLK PGSVEQVSEI
MKLATETGTA IVPQTGNTGL VGGQTPRAGK SDIILSLERM NRIRDVDPVA NVLVADGGAI
LAEVQKAAEA HGRLFPLSLG SEGSCRIGGN LSTNAGGTAV LAYGNMRQLC LGLEVVLPTG
EIWDGLRRLK KDNTGYDLRD LFIGAEGTLG IITGAVLKLF PQPLGHQVAF AGLNSVADAL
GLFNLASSLC GASLTGFELM PRFGVEITTR HIDGVRDPLE AAYPWYVLID ISTSDSAETA
ERMMNGVLEQ GFEAGLVLDA AIASSVAQQK AIWHMRESMS DAQKPEGGSI KHDVSVPVSR
IPHFMAEAEE AVMAAMPGAR ICAFGHMGDG NIHYNISQPI GADKAAFIGR WREMNHIVHG
LVLAHGGSIS AEHGIGQLKR DELAAIRPAI EIELMRRIKR AFDPANIMNP GKVVSVDV
//
