ID A0A1B7LZ54_9MICC Unreviewed; 476 AA.
AC A0A1B7LZ54;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OAV60802.1};
GN ORFNames=A6F49_09915 {ECO:0000313|EMBL:OAV60802.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV60802.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV60802.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV60802.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-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, 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:OAV60802.1}.
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DR EMBL; LXEY01000018; OAV60802.1; -; Genomic_DNA.
DR RefSeq; WP_043057849.1; NZ_LXEY01000018.1.
DR AlphaFoldDB; A0A1B7LZ54; -.
DR STRING; 1837282.A6F49_09915; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000078292; 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; 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 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}.
FT DOMAIN 92..225
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 237..459
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 476 AA; 50418 MW; E651A83730BC2A96 CRC64;
MATPSPGYSI IVKVQAPTTF TATSDLTAVV AEAGAAITAL DIVDASHESN IINLTCNTRG
KEHSRQVKDA IEAVEGFEVL SLSDRTFHMH QGGKLQTVSK VHVRNRDDLS RAYTPGVARV
CKAIAKDPVR ARELTIKRNT IAVVTDGTAV LGLGDIGPAA AMPVMEGKAV LFKQFANVDA
WPVALDTKDT EEIIQIVKAL APAYGGINLE DISAPRCFEI EARLREELDI PVFHDDQHGT
AIVTQAALNN ALKVVNKKIE DVRIVVSGVG AAGHAIIRLL KASGAQHIMA AGRDGVLEPN
TSQRDEHRQW LADNTNTEGF SGSLKEAMVG ADVFIGVSAP NLIDADDVAN MNEGSIIFAM
ANPDPEILPT EASQHAAVVA TGRSDFPNQI NNVLAFPGLF RGLLDAGASD ITEDMLVAAA
DAISETITED ELNPSYVIPS VFNQRVAPAV AAAVAAVAER NGVAPTTTET QDDIDF
//
