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Entry: A0A1B1KVZ8_SERPL
LinkDB: A0A1B1KVZ8_SERPL
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ID   A0A1B1KVZ8_SERPL        Unreviewed;       264 AA.
AC   A0A1B1KVZ8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-FEB-2019, entry version 13.
DE   RecName: Full=Probable L-aspartate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01265};
DE            EC=1.4.1.21 {ECO:0000256|HAMAP-Rule:MF_01265};
GN   Name=nadX {ECO:0000256|HAMAP-Rule:MF_01265,
GN   ECO:0000313|EMBL:ANS44617.1};
GN   ORFNames=Q5A_020975 {ECO:0000313|EMBL:ANS44617.1};
OS   Serratia plymuthica PRI-2C.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1154756 {ECO:0000313|EMBL:ANS44617.1, ECO:0000313|Proteomes:UP000013567};
RN   [1] {ECO:0000313|EMBL:ANS44617.1, ECO:0000313|Proteomes:UP000013567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Serratia sp. PRI-2C {ECO:0000313|Proteomes:UP000013567};
RX   PubMed=22815440; DOI=10.1128/JB.00679-12;
RA   Garbeva P., van Elsas J.D., de Boer W.;
RT   "Draft genome sequence of the antagonistic rhizosphere bacterium
RT   Serratia plymuthica strain PRI-2C.";
RL   J. Bacteriol. 194:4119-4120(2012).
CC   -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent
CC       dehydrogenation of L-aspartate to iminoaspartate.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11788, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.4.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01265};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-aspartate + NADP(+) = H(+) + NADPH + NH4(+) +
CC         oxaloacetate; Xref=Rhea:RHEA:11784, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.4.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01265};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis;
CC       iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous
CC       solution and can decompose to oxaloacetate and ammonia.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
CC   -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01265}.
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DR   EMBL; CP015613; ANS44617.1; -; Genomic_DNA.
DR   RefSeq; WP_006321004.1; NZ_CP015613.1.
DR   EnsemblBacteria; ANS44617; ANS44617; Q5A_020975.
DR   KEGG; sply:Q5A_020975; -.
DR   KO; K06989; -.
DR   OrthoDB; 1670363at2; -.
DR   BioCyc; GCF_000261045:G1EES-4240-MONOMER; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000013567; Chromosome.
DR   GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006742; P:NADP catabolic process; IEA:InterPro.
DR   HAMAP; MF_01265; NadX; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR002811; Asp_DH.
DR   InterPro; IPR020626; Asp_DH_prok.
DR   InterPro; IPR011182; L-Asp_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01958; DUF108; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000013567};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01265};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01265};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01265};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   DOMAIN        8    115       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      164    251       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    216    216       {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     120    120       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     186    186       NAD. {ECO:0000256|HAMAP-Rule:MF_01265}.
SQ   SEQUENCE   264 AA;  27786 MW;  FA959C922AF4D389 CRC64;
     MKNIMMIGYG AMAKEVLSRL PEGVDVGWIV ARAAHHAAID SAFGGKVQAL THPDHCSGLP
     DLVLECASQQ AVAEFGEAVV KRGWSLAVIS TGALADAALQ LRLQQAGRQY QGRVIVLSGA
     VAGMDGLASA REGGLDSVTY QASKSPASWR GSLAEKLIDL DKVSEARVFF EGSAREAARL
     FPANANVAAT IALNGLGMDA TRVRLQVDPH TRRNTHRLQV CGSFGEFHIE LSGNPLASNP
     KTSTLAALSA VQACRRLIDG GFIA
//
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