(data stored in ACNUC1104 zone)

SWISSPROT: D7A404_STAND

ID   D7A404_STAND            Unreviewed;       502 AA.
AC   D7A404;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|RuleBase:RU362049};
GN   OrderedLocusNames=Snov_0491 {ECO:0000313|EMBL:ADH87824.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87824.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87824.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to
CC       iminoaspartate. {ECO:0000256|RuleBase:RU362049}.
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|RuleBase:RU362049};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362049};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|RuleBase:RU362049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       NadB subfamily. {ECO:0000256|RuleBase:RU362049}.
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DR   EMBL; CP002026; ADH87824.1; -; Genomic_DNA.
DR   RefSeq; WP_013165329.1; NC_014217.1.
DR   STRING; 639283.Snov_0491; -.
DR   EnsemblBacteria; ADH87824; ADH87824; Snov_0491.
DR   KEGG; sno:Snov_0491; -.
DR   eggNOG; ENOG4107S3R; Bacteria.
DR   eggNOG; COG0029; LUCA.
DR   HOGENOM; HOG000160476; -.
DR   KO; K00278; -.
DR   OMA; FMERYHP; -.
DR   OrthoDB; 153138at2; -.
DR   BioCyc; SNOV639283:G1GLM-496-MONOMER; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 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:SF2; PTHR42716:SF2; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR00551; nadB; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A404.
DR   SWISS-2DPAGE; D7A404.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   FAD {ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362049};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
FT   DOMAIN        8    372       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      450    474       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   502 AA;  51848 MW;  29A1F3F3DDC956E1 CRC64;
     MSHSPENIVV VGGGVAGLAT ALRLAPMKVT LVVASPLGSD AATGWAQGGI AAAIGDDDRP
     DFHAIDTLTA GAGLSEPHVA RRVAAAAPEA IDWLVGLGTP FDRNANGSLA LGLEAAHSRR
     RIVHADGDGT GRVVLETLAK AARACPSIQV IEAVRATELL LTEGRVAGVA VRDREGRVTA
     LAARAVVLAT GGLGGLYAST TNPLGAVGSG LALAARAGAA LRDMEFVQFH PTAIAAGADP
     MPLATEALRG EGAKLLNARG ERFMAEVPGQ ELAPRDVVAR AIFAQIAQGH GVVLDARLKD
     VERRFPGVVA LCRANGLDPA RAPIPVRPAA HYHMGGIKVD DAGRSTVPGL WACGEVASTG
     LHGANRLASN SLLEALAYAQ WIAADIAGEE AAHSAVPAPV SPRAPSPARA EIRALMDLKV
     GVVRDAANLE AAARWLGELA DRHDDDPSLV ALMVTEAALR REESRGGHFR ADYPLPATLA
     RHSETTLDAL DRREAGEVRR VA
//

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