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Database: UniProt
Entry: A0A1R1D2L1_9BACL
LinkDB: A0A1R1D2L1_9BACL
Original site: A0A1R1D2L1_9BACL 
ID   A0A1R1D2L1_9BACL        Unreviewed;       471 AA.
AC   A0A1R1D2L1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OMF30868.1};
GN   ORFNames=BK133_16435 {ECO:0000313|EMBL:OMF30868.1};
OS   Paenibacillus sp. FSL H8-0548.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF30868.1, ECO:0000313|Proteomes:UP000187405};
RN   [1] {ECO:0000313|EMBL:OMF30868.1, ECO:0000313|Proteomes:UP000187405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF30868.1,
RC   ECO:0000313|Proteomes:UP000187405};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) 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}.
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:OMF30868.1}.
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DR   EMBL; MRTK01000022; OMF30868.1; -; Genomic_DNA.
DR   RefSeq; WP_076337506.1; NZ_MRTK01000022.1.
DR   AlphaFoldDB; A0A1R1D2L1; -.
DR   STRING; 1920422.BK133_16435; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000187405; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd05311; NAD_bind_2_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; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000187405}.
FT   DOMAIN          93..226
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          238..460
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         212
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         237
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   471 AA;  51041 MW;  F6C4E5236A55EBC8 CRC64;
     MSSNMTDGKT IILRLEIDTN LAQFGRAATA IEQAKGDIIA IDVIHTDRNK SLRDLTVKIS
     EHGAAERLTT ALKSLEGIRL VHISDRTFLL HLGGKITVQP KTPIQNRDDL SRVYTPDVAR
     VCQAIFEEPS KAYTLTVKRN MVAVVSDGSA VLGLGNIGPY AAMPVMEGKA MLFKQFADVD
     AFPICLDTQD TEAIIATIIN IAPAFGGINL EDISAPRCFE IEQRLRGVLD IPVFHDDQHG
     TAVVLYAGLL NALKLTGRKL SEARIVVCGI GAAGTACSKM LLAGGAEHIV GVDREGILTA
     NQTYDNAMWQ WYAEHTNSQR QSGSLADALK DADVFIGVSA GGILTRALIE TMAKDPVVFA
     MANPEPEIRP ELAEDIVAVF ATGRSDYPNQ INNVLCFPGI FRGALDSRAT TINEEMKLAA
     AEAIASVISD DELSPMYIVP SVFNNRVVEE VRRRVIQAAQ QSGVSRRQTR E
//
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