ID B9DZP6_CLOK1 Unreviewed; 529 AA.
AC B9DZP6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 79.
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 OrderedLocusNames=CKR_0670 {ECO:0000313|EMBL:BAH05721.1};
OS Clostridium kluyveri (strain NBRC 12016).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH05721.1, ECO:0000313|Proteomes:UP000007969};
RN [1] {ECO:0000313|Proteomes:UP000007969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA Yukawa H.;
RT "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT of Clostridia species.";
RL Submitted (SEP-2005) 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; AP009049; BAH05721.1; -; Genomic_DNA.
DR RefSeq; WP_011989317.1; NC_011837.1.
DR AlphaFoldDB; B9DZP6; -.
DR KEGG; ckr:CKR_0670; -.
DR HOGENOM; CLU_014312_3_0_9; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000007969; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362049};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU362049}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..390
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 529 AA; 59731 MW; C77899E2E83DAE77 CRC64;
MRRYLVDYNE SFVIDQNFDV AIIGAGIAGL YTALMLPKDL KIVILSKKDI EDCDSYLAQG
GIAASIKNDN RELHVKDTIN AGCYVNDLDA VNVLINESQE AIDSLVELGV DFDRDSLGNF
YRSLEGNHSM PRILHVHGDS TGKGIMDILI KNVKEASNIT VITDIFAMDV VDSEKIYKGI
TAYHNDKFFY FNTKFCVVAS GGIGQLFSKT TNVDILTGDG IAMALRAGVN LDNMEYIQFH
PTAFYSKDVK DKLFLISEAV RGEGAVLRNI NEERFMGEYD NRMELAPRDI VARAIKDQMD
KTKTDYVYLD VTMYDKNFLK RRFNTIYSEC KSQGIEMNKD YIPVTPAAHY FMGGIKVDLY
GRTNIENFYA VGECACTGVH GANRLASNSL MEALVFGKRA AVDISCRMKQ KKYLDYEDMN
KIGIKTLFNG FKTEHMKIDF SVLKENLKNF MEDTAGIVRS VDKLKKVLDY INNVLYEIEN
CNFSDIYSME VYNMYQVSGA IVTSILDSKA SIGSNYVEEY SERSLVRQI
//
