ID A0A399FYY4_9ACTN Unreviewed; 866 AA.
AC A0A399FYY4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|RuleBase:RU362049};
DE EC=1.4.3.16 {ECO:0000256|RuleBase:RU362049};
GN ORFNames=NI17_018255 {ECO:0000313|EMBL:UOE18716.1}, NI17_16610
GN {ECO:0000313|EMBL:RII01568.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RII01568.1};
RN [1] {ECO:0000313|EMBL:RII01568.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RII01568.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE18716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE18716.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC first step in the de novo biosynthesis of NAD(+).
CC {ECO:0000256|ARBA:ARBA00029426}.
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000256|ARBA:ARBA00003237}.
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004893}.
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 -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400}.
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DR EMBL; JRUV01000274; RII01568.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE18716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399FYY4; -.
DR STRING; 483545.GCA_001660385_04718; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000265719; 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:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; IPR004393; NadC.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR00551; nadB; 1.
DR NCBIfam; TIGR00078; nadC; 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; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000265719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..410
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 453..530
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT DOMAIN 607..695
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 697..861
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT REGION 519..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 90896 MW; 1E7C75BD47DB3576 CRC64;
MSTSPAPLPL RLTAPEPGWT IEADVVVVGS GIAGLSTALR YVERTRSGRV VLVTKDLLAN
GSTRWAQGGI AAAVDPGDDP LAHLVDTVEA GAGLCDPEAV RLLVDEGPEA LRWLIAQGTA
FDRTESGELS LTREGGHRAD RIAHAGGDAT GAEIERALVD AVRARDRIEL IEHAFVPDLL
LGADDRGGSR VHGITVHVMG EGERDGVGAV RAGAVVLATG GMGQVFASTT NPGVSTGDGL
ALGLRAGAEV QDLEFVQFHP TVLWLGPDAR GRQPLVSEAV RGEGAFLVDV RGRRFMAGAH
ELADLAPRDV VARGIARAMA ETGADHVYLD ARHFGAARWE RRFPTILASC RAHGVDPVTD
LIPVTPAAHY ASGGIRVDHD GRTAVPGLYA VGEVARTGVH GANRLASNSL LEGVVFADRI
AAALAEERPP ATVPARPGRP GPAGLADPAI LPELREIMSR HVGVRREAGG LATAAEALAE
LAARDTADVP PGVPAWQAAN LLTVAWALVR AAARRCETRG SHWRSDHEQP SAEARSRTFV
LDGSGIREER SMRPYTLPAQ LVEELDRITV PEAMRRGAAP GRSGERPAAW HEELVRTALA
EDRSGEQVDV TTVATIPAAQ TRTADVVARR DGVVAGLPVA ELVFRTVCGG VLEVVRHAAD
GDPVKSGDVL MTVTARTRDL LTAERTALNF LTHLSGIATA TRAWVDAVAG TGAAIRDSRK
TLPGLRVLEK YAVRCGGGVN HRFGLADAAL VKDNHVAAAG GVSEAVRAVR ERFPDTPLEV
EVDRIDQIEP ALAAGAEEIL LDNFTVPQLR EAVALVAGRA RLESSGGLTL DRAADVAATG
VDYLAVGALT HSSPALDIAL DLRETP
//
