NADB_SULTO
ID NADB_SULTO Reviewed; 472 AA.
AC Q972D2; F9VNW8;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=L-aspartate oxidase {ECO:0000303|PubMed:18226609};
DE Short=LAO {ECO:0000303|PubMed:18226609};
DE Short=LASPO {ECO:0000303|PubMed:23371294};
DE EC=1.4.3.16 {ECO:0000269|PubMed:18226609, ECO:0000269|PubMed:23371294};
DE AltName: Full=Quinolinate synthase B;
GN Name=nadB {ECO:0000303|PubMed:18226609}; OrderedLocusNames=STK_11960;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=23371294; DOI=10.1007/s00253-013-4688-1;
RA Bifulco D., Pollegioni L., Tessaro D., Servi S., Molla G.;
RT "A thermostable L-aspartate oxidase: a new tool for biotechnological
RT applications.";
RL Appl. Microbiol. Biotechnol. 97:7285-7295(2013).
RN [3] {ECO:0007744|PDB:2E5V}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DOMAIN.
RX PubMed=18226609; DOI=10.1016/j.bbapap.2007.12.012;
RA Sakuraba H., Yoneda K., Asai I., Tsuge H., Katunuma N., Ohshima T.;
RT "Structure of l-aspartate oxidase from the hyperthermophilic archaeon
RT Sulfolobus tokodaii.";
RL Biochim. Biophys. Acta 1784:563-571(2008).
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC first step in the de novo biosynthesis of NAD(+) (PubMed:18226609,
CC PubMed:23371294). Can also use L-asparagine, but not L-phenylalanine,
CC L-glutamate, glycine, L-proline, L-alanine and D-aspartate
CC (PubMed:23371294). {ECO:0000269|PubMed:18226609,
CC ECO:0000269|PubMed:23371294}.
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:0000269|PubMed:18226609, ECO:0000269|PubMed:23371294};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000269|PubMed:18226609, ECO:0000269|PubMed:23371294};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18226609, ECO:0000269|PubMed:23371294};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18226609};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for L-aspartate {ECO:0000269|PubMed:18226609,
CC ECO:0000269|PubMed:23371294};
CC KM=18.1 mM for L-asparagine {ECO:0000269|PubMed:23371294};
CC Vmax=0.98 umol/min/mg enzyme with L-aspartate as substrate
CC {ECO:0000269|PubMed:23371294};
CC Vmax=0.22 umol/min/mg enzyme with L-asparagine as substrate
CC {ECO:0000269|PubMed:23371294};
CC pH dependence:
CC Optimum pH is 8.0 (for L-aspartate oxidation) (PubMed:18226609).
CC Optimum pH is about 10.0. Stable between pH 7.0 and 10.0
CC (PubMed:23371294). {ECO:0000269|PubMed:18226609,
CC ECO:0000269|PubMed:23371294};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Thermostable up to 80
CC degrees Celsius. {ECO:0000269|PubMed:23371294};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18226609,
CC ECO:0000269|PubMed:23371294}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: Folds into three domains: the FAD-binding domain, the capping
CC domain and the C-terminal helical domain.
CC {ECO:0000269|PubMed:18226609}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000023; BAK54476.1; -; Genomic_DNA.
DR RefSeq; WP_010979215.1; NC_003106.2.
DR PDB; 2E5V; X-ray; 2.09 A; A/B=1-472.
DR PDBsum; 2E5V; -.
DR AlphaFoldDB; Q972D2; -.
DR SMR; Q972D2; -.
DR STRING; 273063.STK_11960; -.
DR PRIDE; Q972D2; -.
DR EnsemblBacteria; BAK54476; BAK54476; STK_11960.
DR GeneID; 1459193; -.
DR KEGG; sto:STK_11960; -.
DR PATRIC; fig|273063.9.peg.1352; -.
DR eggNOG; arCOG00572; Archaea.
DR OMA; HCVQWLI; -.
DR OrthoDB; 8547at2157; -.
DR BRENDA; 1.4.3.16; 15396.
DR UniPathway; UPA00253; UER00326.
DR EvolutionaryTrace; Q972D2; -.
DR Proteomes; UP000001015; 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-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; PTHR42716; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Nucleotide-binding;
KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..472
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184412"
FT ACT_SITE 257
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 7..10
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 29
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT BINDING 353..354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18226609,
FT ECO:0007744|PDB:2E5V"
FT SITE 102
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 71..90
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2E5V"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 257..269
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2E5V"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 428..442
FT /evidence="ECO:0007829|PDB:2E5V"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2E5V"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:2E5V"
SQ SEQUENCE 472 AA; 52582 MW; 9B31FAC6FE79801F CRC64;
MIYIIGSGIA GLSAGVALRR AGKKVTLISK RIDGGSTPIA KGGVAASVGS DDSPELHAQD
TIRVGDGLCD VKTVNYVTSE AKNVIETFES WGFEFEEDLR LEGGHTKRRV LHRTDETGRE
IFNFLLKLAR EEGIPIIEDR LVEIRVKDGK VTGFVTEKRG LVEDVDKLVL ATGGYSYLYE
YSSTQSTNIG DGMAIAFKAG TILADMEFVQ FHPTVTSLDG EVFLLTETLR GEGAQIINEN
GERFLFNYDK RGELAPRDIL SRAIYIEMLK GHKVFIDLSK IEDFERKFPV VAKYLARHGH
NYKVKIPIFP AAHFVDGGIR VNIRGESNIV NLYAIGEVSD SGLHGANRLA SNSLLEGLVF
GINLPRYVDS SWEGISTDDG IVHSVRISGN KTLSLKEIRR INWENVGIIR NEEKLVKAIN
TYSSSTQNEA IISYLTALAA EIRKESRGNH FREDYPYKDP NWEKRIYFKL VV
