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Database: UniProt
Entry: A0A257SUG4_9GAMM
LinkDB: A0A257SUG4_9GAMM
Original site: A0A257SUG4_9GAMM 
ID   A0A257SUG4_9GAMM        Unreviewed;       420 AA.
AC   A0A257SUG4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OYV76802.1};
GN   ORFNames=B7Z66_06890 {ECO:0000313|EMBL:OYV76802.1};
OS   Chromatiales bacterium 21-64-14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales.
OX   NCBI_TaxID=1970504 {ECO:0000313|EMBL:OYV76802.1, ECO:0000313|Proteomes:UP000215939};
RN   [1] {ECO:0000313|EMBL:OYV76802.1, ECO:0000313|Proteomes:UP000215939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-64-14 {ECO:0000313|EMBL:OYV76802.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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}.
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:OYV76802.1}.
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DR   EMBL; NCBI01000010; OYV76802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257SUG4; -.
DR   Proteomes; UP000215939; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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; 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.
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}.
FT   DOMAIN          19..152
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          164..400
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        95
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         163
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   420 AA;  44973 MW;  BD67A24D07154610 CRC64;
     MNEETLKAEA LRYHAEPRPG KISVAVTKPC ATRNDLRLAY TPGVAAPVRA IVEDPENAYR
     YTAKGNLVAV ITNGSAVLGL GKVGPLAAKP VMEGKAVLFK VFADLDVFDI EVDADTPQAF
     IDTVVRIAPT FGGINLEDIA APQCFEIEQA LIEQLDIPVF HDDQHGTAII VAAGLLNALE
     LQDKTMETAR IVCLGAGAAG IASMRLLIAM GAKKDHILMV DRQGVLHLGR EDLNPHKWAL
     AADTDRRTLA EALEGADVFV GVSGAGLVSP AMVAVMAPRP IVFALANPDP EIHPEDAHRV
     RDDLIMATGR SDYPNQVNNV LGFPYIMRGA LDVRARGVTQ GMQVAAVHAL RELAREPVPK
     SVLEAYGLER LAYGPEYILP KPVDPRLIHH VAPAVAWAAV QAGVARVAYP AHYPRLEAAG
//
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