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Database: UniProt
Entry: A0A1B8QCE3_9GAMM
LinkDB: A0A1B8QCE3_9GAMM
Original site: A0A1B8QCE3_9GAMM 
ID   A0A1B8QCE3_9GAMM        Unreviewed;       550 AA.
AC   A0A1B8QCE3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   ORFNames=A9306_09455 {ECO:0000313|EMBL:OBX78373.1};
OS   Moraxella atlantae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=34059 {ECO:0000313|EMBL:OBX78373.1, ECO:0000313|Proteomes:UP000092616};
RN   [1] {ECO:0000313|EMBL:OBX78373.1, ECO:0000313|Proteomes:UP000092616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 59586 {ECO:0000313|EMBL:OBX78373.1,
RC   ECO:0000313|Proteomes:UP000092616};
RA   Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome of Moraxella atlantae CCUG 59586.";
RL   Submitted (JUN-2016) 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:OBX78373.1}.
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DR   EMBL; LZNA01000047; OBX78373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8QCE3; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000092616; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092616}.
FT   DOMAIN          11..402
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          452..532
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   550 AA;  61027 MW;  55A2EC3F94025ADA CRC64;
     MTGSDEITHF DVVIVGGGAA GLTLALSLPK HLSVAMLMKD EPLESSTYYA QGGVAAVWAQ
     DDTVDEHIAD TLIAGAGLCH EEAVRFTVEH SREAIEFLLA QGVKFTLDEN SDDLHLTQEG
     GHSRRRIAHV ADATGRAVAT TLLERVRECQ NVTLLDHMVA IDVITTNSLA QHFDAPFTEP
     NRAVGVYVLD TKAHRVLTLS AGFVALACGG VSKAYLYTSN PDIATGDGIA MAWRAGCRVA
     NLEFNQFHPT CLYHPEARSF LLTEALRGEG AYLRLPPCDH HPEGERFMLR FDSRGELAPR
     DIVALTIDFE MKRLGLRHVY LDITHKDPEF VKAHFPTLYA RLLEFGIDIT QDQIPVVPAA
     HYTCGGVVVN QQGQTDVLNL YALGETSFTG LHGANRMASN SLLECFVYAM SAATHIRDSH
     AHAAPSVPMI PTWHIQDNTD QDEAVILLQN WDELRHTMWH YVGIVRSNKR LHRALNRILL
     LKQEMQDYYD SFALNKNLIE LRNLLLVSEL IVRCALRRHE SRGLHYNRDF PQSLPTPADV
     VLTPAVPSAV
//
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