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Database: UniProt
Entry: A0A147HWP7_9SPHN
LinkDB: A0A147HWP7_9SPHN
Original site: A0A147HWP7_9SPHN 
ID   A0A147HWP7_9SPHN        Unreviewed;       525 AA.
AC   A0A147HWP7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   Name=nadB {ECO:0000313|EMBL:NVP31131.1};
GN   ORFNames=HLV41_08750 {ECO:0000313|EMBL:NVP31131.1}, NS258_14965
GN   {ECO:0000313|EMBL:KTW09707.1}, NS319_10895
GN   {ECO:0000313|EMBL:KTT69284.1};
OS   Sphingomonas sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=33051 {ECO:0000313|EMBL:KTT69284.1, ECO:0000313|Proteomes:UP000072867};
RN   [1] {ECO:0000313|Proteomes:UP000072867, ECO:0000313|Proteomes:UP000074410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS258 {ECO:0000313|EMBL:KTW09707.1,
RC   ECO:0000313|Proteomes:UP000074410}, and NS319
RC   {ECO:0000313|EMBL:KTT69284.1, ECO:0000313|Proteomes:UP000072867};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
RN   [2] {ECO:0000313|EMBL:NVP31131.1, ECO:0000313|Proteomes:UP000531581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS-IIF7SWP {ECO:0000313|EMBL:NVP31131.1};
RA   Bijlani S., Singh N.K., Mason C.E., Wang C.C., Venkateswaran K.;
RT   "Draft Genome Sequences of Sphingomonas sp. Isolated from the International
RT   Space Station.";
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CC       {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|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         ECO:0000256|RuleBase:RU362049};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004950, ECO:0000256|RuleBase:RU362049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC       subfamily. {ECO:0000256|ARBA:ARBA00008562,
CC       ECO:0000256|RuleBase:RU362049}.
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:KTT69284.1}.
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DR   EMBL; LDTD01000073; KTT69284.1; -; Genomic_DNA.
DR   EMBL; LDTC01000129; KTW09707.1; -; Genomic_DNA.
DR   EMBL; JABYQV010000005; NVP31131.1; -; Genomic_DNA.
DR   RefSeq; WP_058717842.1; NZ_LDTD01000073.1.
DR   AlphaFoldDB; A0A147HWP7; -.
DR   STRING; 33051.SB4_18545; -.
DR   PATRIC; fig|33051.3.peg.3378; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000072867; Unassembled WGS sequence.
DR   Proteomes; UP000074410; Unassembled WGS sequence.
DR   Proteomes; UP000531581; Unassembled WGS sequence.
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; 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   NCBIfam; TIGR00551; nadB; 1.
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   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 2.
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.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362049};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU362049}.
FT   DOMAIN          5..384
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          434..513
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        282
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   525 AA;  57917 MW;  F33C06C515151889 CRC64;
     MTDSDILIVG SGAAGLTAAL NLADRFKVTV LAKGKLNEGS TAWAQGGIAA VLEPGDTFES
     HIEDTMVAGA GLNDRATVEF VVENAPAAIE RLQKLGVPFA TEGNMLHLTR EGGHSHRRIV
     HVADATGWAV LDALLRAAEA HPNITLVPDQ VAIDLATSRH EMRYSGAGHV WGIYAVDRRT
     GRVVVHKARA TILATGGAGR TYQFSTAPKG ATGDGIAMAW RAGARVSNME FMQFHPTCLY
     NTQVKNFLIT EAVRGEGGHL KIPETGHRFM PDFDARAELA PRDIVARAID HEIKRLGLDY
     VHLDISHQSP AFIREHFPNI HEKLLSLGID MTVQPIPVVP AQHYTCGGVI VDRDGRTDLP
     GLYAAGEVTQ SGLHGANRLA SNSLLECFVY GEACANHIAA HWDDLPPPPA IRPWDESRVT
     DSDEEVVIKQ NWTEIRRFMW NYVGIVRTTK RLERAQHRIR MLTDEINDYY GHFRVTPDLI
     ELRNLLQTAE LIVRCALHRK ESRGLHYTRD YPDTLPEAVD TILIP
//
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