UniProt: D4M7Z4

Database: UniProt
Entry: D4M7Z4_9BACT

LinkDB:  D4M7Z4_9BACT 
Original site:  D4M7Z4_9BACT

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (2)   
All databases (14)   

Download RDF

ID   D4M7Z4_9BACT            Unreviewed;       504 AA.
AC   D4M7Z4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN   ORFNames=SY1_06080 {ECO:0000313|EMBL:CBL27989.1};
OS   Fretibacterium fastidiosum.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC   Fretibacterium.
OX   NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL27989.1, ECO:0000313|Proteomes:UP000008957};
RN   [1] {ECO:0000313|EMBL:CBL27989.1, ECO:0000313|Proteomes:UP000008957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGP1 {ECO:0000313|EMBL:CBL27989.1,
RC   ECO:0000313|Proteomes:UP000008957};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT   "The genome sequence of Synergistetes sp. SGP1.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL27989.1, ECO:0000313|Proteomes:UP000008957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGP1 {ECO:0000313|EMBL:CBL27989.1,
RC   ECO:0000313|Proteomes:UP000008957};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004950}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC       subfamily. {ECO:0000256|ARBA:ARBA00008562}.
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; FP929056; CBL27989.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4M7Z4; -.
DR   KEGG; sbr:SY1_06080; -.
DR   PATRIC; fig|651822.3.peg.2095; -.
DR   HOGENOM; CLU_014312_8_1_0; -.
DR   BioCyc; FFAS651822:G13GF-376-MONOMER; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000008957; Chromosome.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic 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   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CBL27989.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008957}.
FT   DOMAIN          6..376
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          471..495
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   504 AA;  54010 MW;  CF12417F0618FA34 CRC64;
     MSRHSVAIAG SGLAALATAA RLHELGVRDI ALYANGFGGT PFIAAINFVL PDNPYGDTPE
     LYCTDMLHAG YDIADRETVR RMTSRTADGY ELLCRWGVTF ARNEDGTLKR RHVSGHTHPR
     SLCQTTRLIG AEILEAMLTR LEAAGIEVHR RCPVAGLLTR GGRIEGFTVL QDGEPHNVYA
     PATVAAWGGV GGLLGPTTYP GDVQGNTLGM AKEAGATMID MEFLEFEPMV MMDPPGTVGE
     PAPTAMLGEG GHLLNSRGER FLLSVRPQGE GGAPKSLINR EAWKQVQSGK GSPRGGVFLD
     LRHIDRAVLQ SYPWFYDRLM KNGCDPNRQL LEVGPMAHSF SGGIRVDADY RSDVQGLYAV
     GEACGGLHGA CRCAGNAASQ AVLSGLLCAE GIAKEGGLDR AISPHPLRCT QDATLRGKVL
     PKLRGIAAHA LGIYRNGPDL EAARSAVKAI LDEPVTARDD LTRQSALAIL TIAEAALNRK
     ESRGTHSRLD FPETDPAFQR EFTL
//

DBGET integrated database retrieval system