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Database: UniProt
Entry: A0A0Q5NHB3_9BURK
LinkDB: A0A0Q5NHB3_9BURK
Original site: A0A0Q5NHB3_9BURK 
ID   A0A0Q5NHB3_9BURK        Unreviewed;       542 AA.
AC   A0A0Q5NHB3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:KQR74081.1};
GN   ORFNames=ASG35_19970 {ECO:0000313|EMBL:KQR74081.1};
OS   Burkholderia sp. Leaf177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR74081.1, ECO:0000313|Proteomes:UP000051826};
RN   [1] {ECO:0000313|EMBL:KQR74081.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74081.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR74081.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74081.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:KQR74081.1}.
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DR   EMBL; LMPF01000025; KQR74081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5NHB3; -.
DR   OrthoDB; 3314528at2; -.
DR   Proteomes; UP000051826; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051826}.
FT   DOMAIN          73..253
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          263..514
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         238
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         239
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         262
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   542 AA;  59540 MW;  BA71938411F0FEDE CRC64;
     MQKPIELSGR DILRDPRLNK GSAFTEEERR KYHLEGLLPP GSSSLELQVA RTHTELAALD
     SDLQKYLLLS DLQARNETLF YATIMSDPAT FMPLVYTPTV GEACQKFNHI FRATRGMYVP
     ISARGRVKEL LQNWPEKEVR FIVVTDGERI LGLGDLGVGG MGIPIGKLSL YTACAGVPPQ
     YCLPVMLDVG TNNRDLLDDP LYLGLRQERV RGDEYHAFVN EFVEAALELH PQCCVQWEDF
     ANFNAVPLLA RYKDKICTYN DDIQGTAAVA LAGIFAALHI SKQKLVDQRF LFLGGGSAGT
     GIAELISQAM VLEGLTIDEA RARNALFDVN GLMVKSRGDL VDFQKPFAVD HAPVDNFTDA
     VKALKPTGII GVSTVPKLFN QHVIEAMAEI NDRPIIFPYS NPTSRSECTA EEAYKWSSGR
     AIFASGSPFP PVEIEGRTFV PGQGNNVYIF PALGMAVFAT QASRVTDEMF IAAAKAVAEQ
     VSEASLATGL IYPPQSKIFE ASLHVAVRVA ECIFDNDLAR VPRPDDITAL IRDCAYKPAY
     TL
//
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