GenomeNet

Database: UniProt
Entry: D0W9M2_NEILA
LinkDB: D0W9M2_NEILA
Original site: D0W9M2_NEILA 
ID   D0W9M2_NEILA            Unreviewed;       378 AA.
AC   D0W9M2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EEZ75680.1};
GN   ORFNames=NEILACOT_04234 {ECO:0000313|EMBL:EEZ75680.1};
OS   Neisseria lactamica ATCC 23970.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546265 {ECO:0000313|EMBL:EEZ75680.1, ECO:0000313|Proteomes:UP000003843};
RN   [1] {ECO:0000313|EMBL:EEZ75680.1, ECO:0000313|Proteomes:UP000003843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23970 {ECO:0000313|EMBL:EEZ75680.1,
RC   ECO:0000313|Proteomes:UP000003843};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:EEZ75680.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACEQ02000013; EEZ75680.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0W9M2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000003843; 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; 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; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..306
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   ACT_SITE        197
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   378 AA;  40626 MW;  9835F9AF81B04E19 CRC64;
     MVTDAPSAIR WLIGLGMTFD LANGADSNGM LSRKRAGGTT VPRILSYRDF TGLEMMRVLR
     EAVELDENIT QLNRHPAIEL LSDEHGRCVG AILYDLEKRS LVLVHAKAVV LATGGSGRLH
     LQGFATSNHY GATADGLVMA YRIGAKLRDV DSFQYHPTGV AHPPHLAGAL ISEAVRSAGT
     KLVNGLGERF VDELQPRDVV AAAILRECRE GRGVVRDGQV GVFLDTPRLI ANDPDVLNRL
     VTLGHVAHKC GIDPAVEPVM IHPTLHYQNG GVEINGDGAT CVEGLYCAGE VTGGIHGRNR
     LMGNALLDII SFGRRAGKAA ANCGLPLKKV RGGVGHVHDL QREMTRAGLT GDIKAPILYP
     DYGKFDLREH AGLQEQQL
//
DBGET integrated database retrieval system