ID U2X4K6_GEOKU Unreviewed; 405 AA.
AC U2X4K6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:GAD13627.1};
GN ORFNames=GBL_1844 {ECO:0000313|EMBL:GAD13627.1};
OS Geobacillus kaustophilus GBlys.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1337888 {ECO:0000313|EMBL:GAD13627.1, ECO:0000313|Proteomes:UP000016424};
RN [1] {ECO:0000313|Proteomes:UP000016424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBlys {ECO:0000313|Proteomes:UP000016424};
RA Doi K., Mori K., Martono H., Nagayoshi Y., Fujino Y., Tashiro K.,
RA Kuhara S., Ohshima T.;
RT "Draft Genome Sequence of Geobacillus kaustophilus GBlys, a Lysogenic
RT Strain with Bacteriophage phiOH2.";
RL Genome Announc.1:e00634-13(2013).
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}.
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:GAD13627.1}.
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DR EMBL; BASG01000015; GAD13627.1; -; Genomic_DNA.
DR RefSeq; WP_011231030.1; NZ_BASG01000015.1.
DR AlphaFoldDB; U2X4K6; -.
DR Proteomes; UP000016424; 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 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 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}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..385
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 160
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 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 405 AA; 42847 MW; 1F0CDC958C661C3D CRC64;
MEHLRERALL VHRQARGKLS VEVKVPVVNA NDLSLIYSPG VAEPCKEIYV DQDEMYNYTV
KGNFVAVVSN GTAVLGLGNI GARAALPVME GKAALFKAFA GIDAVPLCLD TEDPEQIIQT
VKLLEPAFGG INLEDIAAPA CFVIEERLRQ EMAIPVFHDD QHGTAIVVAA GLTNALKVVG
KQLADCRVVI NGAGAAGVAI AKLLLSIGVG ELIVCDTKGA IYEGRSHGMN AIKEEIARQT
NHRRISGTLA DVIQGADVFI GVSVAGALTP AMVRTMNRGA VVFALANPVP EIMPDEAKAA
GAAVVATGRS DLPNQVNNVL AFPGIFRGAL DVRATQINEA MKIAAAEAIA GLIQPEELTE
EYVIPNPFDR RVVEAVASAV ARAAMETGVA RVKEKVEEQN RVREG
//
