ID I2NNF7_9PAST Unreviewed; 555 AA.
AC I2NNF7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
GN ORFNames=HMPREF1054_1146 {ECO:0000313|EMBL:EIG27368.1};
OS Haemophilus paraphrohaemolyticus HK411.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095743 {ECO:0000313|EMBL:EIG27368.1, ECO:0000313|Proteomes:UP000003345};
RN [1] {ECO:0000313|EMBL:EIG27368.1, ECO:0000313|Proteomes:UP000003345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK411 {ECO:0000313|EMBL:EIG27368.1,
RC ECO:0000313|Proteomes:UP000003345};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-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:EIG27368.1}.
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DR EMBL; AJMU01000018; EIG27368.1; -; Genomic_DNA.
DR RefSeq; WP_005708028.1; NZ_AJMU01000018.1.
DR AlphaFoldDB; I2NNF7; -.
DR PATRIC; fig|1095743.3.peg.301; -.
DR eggNOG; COG1053; Bacteria.
DR OrthoDB; 9148689at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000003345; Unassembled WGS sequence.
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: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 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; 2.
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}.
FT DOMAIN 13..402
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 464..546
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
SQ SEQUENCE 555 AA; 61902 MW; 3CDF9B68B8EA6246 CRC64;
MPNIQITQTL KTDLLIVGSG IGGLSCSVEA HKKGINHILI TKTQLGSGAS FFPLKASLGI
QVTGEEHDKD LFQQDIERVA QGMNNPEIVK AYIEDSPQAV ELLNEIGFYP WKRNDNRPAC
FAKHARPIYL INEWQKARKN AEVIIAQQNT TTLFENASLV YIATENHHVV GAVFAYQNPE
KNGRKIVYFY VQTSTIILAS GGIAGLYKDN LYPADVIGST HFLALQAGAR LTNLEFIQFI
PSFIAPKYKV LFGEHTLKYC TAVTDKNGNS LFPDLSAEEF TQMVAERSAY APFSVDFDCV
KFDLRIMQYL LETPEEQGVY LHYSPKLYQD QTEFYRVYLD WLKADAGIDL LTDRVSIAPF
AHSCNGGIEI DTNAESAVQG LFAVGEVSSC IEGANRLGGN SVGGSLVFAK RAMAKIQQDL
TACSASAINE QAVENAKNLA EQALNRLHNE NADNTLTASQ VLSEIRQAMT KFANVYRTEE
NLCKLQEKLD RLEQDFDPIE NADFQGIEIF YGLKTAQAVV NAMLARKESR GSHYRADYPE
KSERIYRQMM SKMID
//
