ID I9NB54_RHILT Unreviewed; 478 AA.
AC I9NB54;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EJB03962.1};
GN ORFNames=Rleg9DRAFT_2806 {ECO:0000313|EMBL:EJB03962.1};
OS Rhizobium leguminosarum bv. trifolii WSM597.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=754764 {ECO:0000313|EMBL:EJB03962.1, ECO:0000313|Proteomes:UP000005092};
RN [1] {ECO:0000313|EMBL:EJB03962.1, ECO:0000313|Proteomes:UP000005092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM597 {ECO:0000313|EMBL:EJB03962.1,
RC ECO:0000313|Proteomes:UP000005092};
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., Held B., 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 WSM597.";
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; JH719381; EJB03962.1; -; Genomic_DNA.
DR RefSeq; WP_003588184.1; NZ_JH719381.1.
DR AlphaFoldDB; I9NB54; -.
DR HOGENOM; CLU_017779_4_1_5; -.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000005092; 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; 50625 MW; 28EF243AD95A4237 CRC64;
MSSTGISTEL LDRFAAIVGD RYALRGEADL APHLIENRGL YHGSSPLLLK PGSVEDVSAI
MKLATETGTA IVPQTGNTGL VGGQTPRAGK SDIILSLERM NRIRDVDPVA NVLVADGGAI
LADVQKAAEA HGRLFPLSLG SEGSCRIGGN LSTNAGGTAV LAYGNMRQLC LGLEVVLPTG
EIWDGLRRLK KDNTGYDLRD LFIGAEGTLG IITGAVLKLF PQPLGHQVAF AGLNSVADAL
GLFNLASSLC GTSLTGFELM PRFGVEITTR HIDGVRDPLQ AAYPWYVLID ISTSDSAETA
ERMMNGVLEQ GFAAGLVLDA AIASSVAQQQ AIWHMRESMS DAQKPEGGSI KHDVSVPVSR
IPHFMAEAAD AVLAAMPGAR ICAFGHMGDG NIHYNISQPV GADKAAFIGR WREMNHIVHG
LVLAHGGSIS AEHGIGQLKR DELAAIRPAI EIELMRRIKR AFDPANIMNP GKVVSLEI
//
