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Database: UniProt
Entry: A0A3D8M9N6_9ALTE
LinkDB: A0A3D8M9N6_9ALTE
Original site: A0A3D8M9N6_9ALTE 
ID   A0A3D8M9N6_9ALTE        Unreviewed;       563 AA.
AC   A0A3D8M9N6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:RDV26696.1};
GN   ORFNames=DXV75_06840 {ECO:0000313|EMBL:RDV26696.1};
OS   Alteromonas aestuariivivens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1938339 {ECO:0000313|EMBL:RDV26696.1, ECO:0000313|Proteomes:UP000256561};
RN   [1] {ECO:0000313|Proteomes:UP000256561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52655 {ECO:0000313|Proteomes:UP000256561};
RA   Zhang J., Du Z.-J.;
RL   Submitted (AUG-2018) 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:RDV26696.1}.
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DR   EMBL; QRHA01000004; RDV26696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8M9N6; -.
DR   OrthoDB; 3314528at2; -.
DR   Proteomes; UP000256561; 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   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; IPR015884; Malic_enzyme_CS.
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:SF34; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000106-3}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256561}.
FT   DOMAIN          79..259
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          269..529
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         245
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         268
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         416
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         460
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   563 AA;  63069 MW;  666943F598762EC8 CRC64;
     MPEESNRYLY IPHSGPSLLE TPLLNKGSAF TARERAEFNL TGLLPPRYET IEEQVERAYM
     QYSSFEETIN KHIYLRAIQD NNETLYYRLI QSHIDEMMPI IYTPTVGDAC EQFSDIYRSS
     RGLFLSWEER DQLDDIVRNA TKRKVKVIVV TDGERILGLG DQGIGGMGIP IGKLSLYTAC
     GGISPAYTLP VMLDVGTNNQ KLLDDPMYMG ARHPRIGQQE YDEFIERFIK AVTRRWPDVM
     IQFEDFAQPN AMPILNRYRE QICCFNDDIQ GTAAVTLGTI LAACRMKKQT LSEMKVVFVG
     AGSAGCGIAE MLIQQMCHEG LSDEQARKQV FMVDRYGLVC EGMDGLRDFQ QNLQQSAEDI
     ADWSYSGDYP SLLDVMNCAQ PDVLIGVSGQ PGLFTEQVIR AMKQYCDLPI IFPLSNPSRQ
     VEARPEQVIE WTEGEVIIAT GSPFKPVEYN GKRYPVAQCN NSYIFPGIGL GVLASKASLI
     SDEMLMAASN ALADASPLAN HGSGELLPPL TEIASLSKRI AFAVAKVAMQ QELALELSDE
     ALEESIERNF WTPQYRPYKR VSI
//
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