ID J6HBR8_9FIRM Unreviewed; 535 AA.
AC J6HBR8; V9HUL7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE AltName: Full=Quinolinate synthase B {ECO:0000256|ARBA:ARBA00030386};
GN ORFNames=HMPREF1143_1828 {ECO:0000313|EMBL:EJU22565.1},
GN HMPREF9630_01909 {ECO:0000313|EMBL:EHL16337.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU22565.1, ECO:0000313|Proteomes:UP000005244};
RN [1] {ECO:0000313|EMBL:EHL16337.1, ECO:0000313|Proteomes:UP000017818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM2 {ECO:0000313|EMBL:EHL16337.1,
RC ECO:0000313|Proteomes:UP000017818};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacteriaceae bacterium CM2.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EJU22565.1, ECO:0000313|Proteomes:UP000005244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU22565.1,
RC ECO:0000313|Proteomes:UP000005244};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562}.
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:EJU22565.1}.
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DR EMBL; AFZF02000004; EHL16337.1; -; Genomic_DNA.
DR EMBL; ALNK01000021; EJU22565.1; -; Genomic_DNA.
DR RefSeq; WP_009526710.1; NZ_JH815225.1.
DR AlphaFoldDB; J6HBR8; -.
DR PATRIC; fig|796939.3.peg.1427; -.
DR HOGENOM; CLU_014312_8_0_9; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000005244; Unassembled WGS sequence.
DR Proteomes; UP000017818; Unassembled WGS sequence.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
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 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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000005244}.
FT DOMAIN 10..384
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 430..517
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 535 AA; 59349 MW; 678DCF8D40808F86 CRC64;
MVIECKEKCD VLVIGAGIAG ISAAIQAAKC GSSVVLTSST AIFSGSSFFP GTWGLGLIGP
EDEKDEADLE ESIARVGCGM TKPEIVKTFV HNINPSIYDL ESRGVKLRTA EKQDEKEFIP
CFDHKRRNWN GLEAESMRAV FKKELLEYKV KLCPYYEALE LIKNDKRVCG AVFGHKDAIL
AIRSKAVILA TGGYGGLFKN YLTTSDIMGM GHAIALRAGA SLINMEFMQM MPGFISPSPK
TVFNEKTFRF SSFSDDKGNN IFKNIQDYTE LLEQRSTHGP FTSACMDREI DFIIAKEELK
GGVYVRYSDE MKNNPPEFIK TYFEWLKDKK GLTFNDTVSV GIFAHAANGG IKIESDASTE
VSGLYACGEV TGGMHGADRI GGLSSANGLV FGRIAGNSAA IDSNTETISD EKIILKAHYV
FDYSSKLAML RKIMTENAMI SRNEIGLNKA INFCKQTLEE INRSTENLSD KAKVIEYYRL
SANLFTAMAV LKPAILRKES RGSHYREDYP EIIKSEDKRI CIFEKDGKIK AMYER
//
