ID F9ZG29_9PROT Unreviewed; 532 AA.
AC F9ZG29;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 ORFNames=NAL212_1014 {ECO:0000313|EMBL:ADZ25931.1};
OS Nitrosomonas sp. AL212.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ25931.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ25931.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ25931.1,
RC ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; CP002552; ADZ25931.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZG29; -.
DR STRING; 153948.NAL212_1014; -.
DR KEGG; nit:NAL212_1014; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_0_4; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001629; 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; 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001629}.
FT DOMAIN 7..390
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 437..517
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 449..476
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 288
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 532 AA; 59203 MW; FCA01240723EFAA2 CRC64;
MTDNNYDTLI IGSGLAGFSL ALHLAQHQKV CIVTKQAAES GASSWAQGGI AAALSNEDSP
SQHVQDTLIA GSGLCDEGIT RFVTENAADA IHWLIAQGVI FTYDQTSETG YHLTQEGGHS
TRRIIHSGDA TGKAVQQALI QKIRLHPNIT VLEHHIAIDL ITDDRLTDST KDRNKRCIGA
YILDKKKDKV LSFAAQNTVL ATGGASKVYL YTTNPDTATG DGIAMGWRAG CRIANMEFIQ
FHPTCLYHPH AKSFLISEAV RGEGGLLKLP NGERFMLWHD QRGELAPRDI VARAIDFEMK
KRGLDCVYLD ISHKPENFLK EHFPTIYARC LKLGIDITKE PIPVVPAAHY TCGGVITDNH
GKTDLSNLYA IGETAHTGLH GANRLASNSL LECLVLAQTA GSDIISQPTN ELPKLPDWDE
SRVTDADEEI VIAHNWDELR RFMWNYVGIV RTTKRLQRAQ HRIELLREEI DEYYTNFRVT
SDLLELRNLV DSADLIVRCA LQRHESRGLH YSKDYPDTLP LAENTVLKRE IR
//
