ID   R0EF23_CAUVI            Unreviewed;       524 AA.
AC   R0EF23;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Succinate dehydrogenase/fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:ENZ84023.1};
DE   Flags: Precursor;
GN   ORFNames=OR37_00531 {ECO:0000313|EMBL:ENZ84023.1};
OS   Caulobacter vibrioides OR37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ84023.1, ECO:0000313|Proteomes:UP000013063};
RN   [1] {ECO:0000313|EMBL:ENZ84023.1, ECO:0000313|Proteomes:UP000013063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR37 {ECO:0000313|EMBL:ENZ84023.1,
RC   ECO:0000313|Proteomes:UP000013063};
RX   PubMed=23792749;
RA   Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA   Palumbo A.V., Brown S.D.;
RT   "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT   Tolerant to Heavy Metals.";
RL   Genome Announc. 1:0-0(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC         Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00029281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC         Evidence={ECO:0000256|ARBA:ARBA00029281};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ENZ84023.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APMP01000001; ENZ84023.1; -; Genomic_DNA.
DR   RefSeq; WP_004615620.1; NZ_APMP01000001.1.
DR   AlphaFoldDB; R0EF23; -.
DR   STRING; 1292034.OR37_00531; -.
DR   PATRIC; fig|1292034.3.peg.528; -.
DR   eggNOG; COG1053; Bacteria.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000013063; Unassembled WGS sequence.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR005288; NadB.
DR   PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR   PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          10..216
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          423..495
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          479..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  55453 MW;  3E7752F39F67B4DB CRC64;
     MSEPLSLATD VLVIGGGLAG AWAAVAAAQA GADVVLVDKG YCGTSGVTAT AGPGHWWVPP
     ERREAAVADR VQRALGLGDP EWMRRILDLT WTSLPKLSAY YDFSTDEAGQ VQHRALRGPE
     YMAAMRAYAL ASGARILDHH PALQLLRHGD GSIAGATGLS LRGETPWTIR AGAVVIATGG
     VAFASRLLGA ATNTGDGLLM GAEAGADLSG MELSNYYTPS VAGTNMARSM AYSFARWFDA
     DDNELDIPNG PDVTPHLARA LLRGPLFCRL DRVPEDIRAI MPQVQPNFVL PFDRMGIDAY
     RDRFEVTLHA EGTVRGIGGL RVDDQDCQTA VSGLYVAGDA ASRELVTGAI SGGGAVNSSW
     ALSSGQWAGA AAARRARALG ARADALVIAT GQAGLSPRRK AGDFDAAGAI QAVREELNAY
     DKNIFRRGEA LTASLERLDG VWRELSDHGQ AKGRAALRLR EAAALVAAGR WSKAAALARR
     ESRGMHRRED APAPDARLAS RQRAQGLDRV FTRFETPPAQ AEVA
//