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Database: UniProt
Entry: A0A2A3XD14_9GAMM
LinkDB: A0A2A3XD14_9GAMM
Original site: A0A2A3XD14_9GAMM 
ID   A0A2A3XD14_9GAMM        Unreviewed;       559 AA.
AC   A0A2A3XD14;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:PCC21559.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:PCC21559.1};
GN   ORFNames=CIK78_05425 {ECO:0000313|EMBL:PCC21559.1};
OS   Halomonas sp. JB37.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=2024405 {ECO:0000313|EMBL:PCC21559.1, ECO:0000313|Proteomes:UP000217454};
RN   [1] {ECO:0000313|EMBL:PCC21559.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB37 {ECO:0000313|EMBL:PCC21559.1};
RX   PubMed=28644126;
RA   Bonham K.S., Wolfe B.E., Dutton R.J.;
RT   "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL   Elife 6:e22144-e22144(2017).
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:PCC21559.1}.
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DR   EMBL; NRGW01000001; PCC21559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3XD14; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000217454; 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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
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:SF32; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:PCC21559.1}.
FT   DOMAIN          79..259
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          269..525
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         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   559 AA;  61910 MW;  4519CE62687C05F0 CRC64;
     MTTQSKRPLY LPYAGPSLLE MPLLNKGSAF TQQERLAFNL IGLLPQKVET IDDQLARVYR
     QYQQCHSDLE KHIHLRAIQD DNETLYFRLV SQHLEEMLPI IYTPTVGQAC QEFSNIYRNH
     RGLFISYPDR EHMDDILRSA TKDNVKVIVV TDGERILGLG DQGIGGMGIP IGKLALYTAC
     GGISPAYTLP IMIDVGTNNK ALLDDPMYMG WRHERVGQEE YDAFMAEFIA AVKRRWPNVL
     LQFEDFAQAN AVPLLERYRD ELCCFNDDVQ GTASVVVGTL MAACQAREET IAQQRVVFVG
     GGSAGCGIAE QVVVAMEAEG LTESEARARI YIVDRDGLMT NDQAWQRDFQ RRLAHDATLV
     AHWNGQGLEE TIAQIKPTVL IGVCGQRGIF TEQVVRTMHA GCEHPVIMPL SNPTSQAEAV
     PEDVIRWTDG QALVATGSPF APVVYNGRTY AIAQCNNAYI FPGIGLGVIA ASATRITDEM
     LMSASRALAR EAPLVKDGKG ALLPPLSRIR EISKSIAFEV AAQAQQNGVA LQTSGTTLRE
     LIDKASWSPD YRTYRRRAF
//
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