ID A0A0Q2LHE4_MYCGO Unreviewed; 548 AA.
AC A0A0Q2LHE4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Malate oxidoreductase {ECO:0000313|EMBL:KQH75194.1};
GN ORFNames=AO501_00140 {ECO:0000313|EMBL:KQH75194.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH75194.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH75194.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH75194.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) 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:KQH75194.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKTM01000383; KQH75194.1; -; Genomic_DNA.
DR RefSeq; WP_055581753.1; NZ_LKTM01000383.1.
DR AlphaFoldDB; A0A0Q2LHE4; -.
DR STRING; 1778.A9W97_14070; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000051677; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT DOMAIN 73..255
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 265..522
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
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 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 548 AA; 59610 MW; 83BDE231C57851F8 CRC64;
MSDACVPRFP EALSTPSLNR GVGFTHEQRR RLGLTGRLPS AVLTLDQQAD RVWHQLQTMA
TDLGRNLLLE QLHYRHELLY YKVLTDHLPE LMPVVYTPTV GEAIQRFSDE YRGQRGLFLS
IDEPDEIADA FATLGQGPDD IDLIVCTDAE AILGIGDWGV GGIQITVGKL ALYTAGGGID
PRRCLAVSLD VGTDNEQLLQ DPFYLGNRHA RRRGDQYDDF IRRYIETAHR FFPQAILHFE
DFGPANARKV LQTYGENYLV FNDDMQGTGA VVLAAVYGGC RVTGSPLRDQ RIVVFGAGTA
GLGVADQIRE AMIADGATPE QATSQIWPID RQGLLFDDMD DLRDFQVPYA KNREGLGVAA
DQHVGLVDAI KLAAPTVLLG CSAVHGAFTR EAVEAMTAAC ERPMIFPLSN PTSRMEAMPA
DLVQWSGGRA LVTTGSPMAP VVHEGTTYTI GQANNVLVFP GIGLGIIVAG ARRLTQSMLH
ASAKAVAQQA DPVAPGDSLL PDVQNLRDIS AKVAEAVYHA AVDDGVATRT YDDVRQAVLD
RMWSPVYD
//
