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Database: UniProt
Entry: A0A1F2P2U6_9EURY
LinkDB: A0A1F2P2U6_9EURY
Original site: A0A1F2P2U6_9EURY 
ID   A0A1F2P2U6_9EURY        Unreviewed;       261 AA.
AC   A0A1F2P2U6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   16-JAN-2019, entry version 11.
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   ORFNames=SBU_001497 {ECO:0000313|EMBL:OFV65569.1};
OS   Candidatus Syntrophoarchaeum butanivorans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; ANME-2 cluster; Candidatus Syntrophoarchaeum.
OX   NCBI_TaxID=1839936 {ECO:0000313|EMBL:OFV65569.1, ECO:0000313|Proteomes:UP000185779};
RN   [1] {ECO:0000313|EMBL:OFV65569.1, ECO:0000313|Proteomes:UP000185779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BOX1 {ECO:0000313|EMBL:OFV65569.1};
RA   Laso-Perez R., Richter M., Wegener G., Musat F.;
RT   "Microbial consortia oxidize butane by reversing methanogenesis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OFV65569.1}.
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DR   EMBL; LYOR01000010; OFV65569.1; -; Genomic_DNA.
DR   PATRIC; fig|1839936.3.peg.1521; -.
DR   UniPathway; UPA00253; UER00456.
DR   Proteomes; UP000185779; Unassembled WGS sequence.
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; IPR022487; Asp_DH_arc.
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.
DR   TIGRFAMs; TIGR03855; NAD_NadX; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000185779};
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   ECO:0000313|EMBL:OFV65569.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01265};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185779}.
FT   DOMAIN        8    119       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      162    247       DUF108. {ECO:0000259|Pfam:PF01958}.
FT   ACT_SITE    212    212       {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     122    122       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01265}.
FT   BINDING     182    182       NAD. {ECO:0000256|HAMAP-Rule:MF_01265}.
SQ   SEQUENCE   261 AA;  28073 MW;  91C5471F1E812030 CRC64;
     MLRIGIIGCG AIAEAIVKGS SSLDRIKITG LYDRHPEKVS YLSGLLREPP EALTFDDMLG
     VCDLIIEAAS QGAVKEFVPP ALEAGKDVMI MSVGALGDQE LLDRIKRIAE ANNCKIYIPS
     GAIAGVDGVK AAAGSKIKRV RLTTRKPPRA FGVENEENAM HERVLFEGPA REAVKLFPAN
     VNVSLTLSLA GIGPDRTEVR IIQDPSIDLN IHEVEVEGDF GRMHLRFENL PSPSNPKTSF
     LAALSAIALI KRVSEPIEVG T
//
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