ID E4RNX9_HALHG Unreviewed; 410 AA.
AC E4RNX9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Malic protein NAD-binding protein {ECO:0000313|EMBL:ADQ13669.1};
GN OrderedLocusNames=Halsa_0180 {ECO:0000313|EMBL:ADQ13669.1};
OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ13669.1, ECO:0000313|Proteomes:UP000007434};
RN [1] {ECO:0000313|EMBL:ADQ13669.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT "Complete sequence of Halanaerobium sp. sapolanicus.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ13669.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX PubMed=21602336; DOI=10.1128/JB.05209-11;
RA Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT Halanaerobium hydrogenoformans.";
RL J. Bacteriol. 193:3682-3683(2011).
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}.
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DR EMBL; CP002304; ADQ13669.1; -; Genomic_DNA.
DR RefSeq; WP_013404775.1; NC_014654.1.
DR AlphaFoldDB; E4RNX9; -.
DR STRING; 656519.Halsa_0180; -.
DR KEGG; has:Halsa_0180; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000007434; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; 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 Reference proteome {ECO:0000313|Proteomes:UP000007434}.
FT DOMAIN 15..148
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 160..383
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 36
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 133
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 159
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 410 AA; 44598 MW; 1DE667B34066F9EE CRC64;
MNLKEEALKL HKDNLGKLMI KSKVEVKDEH DLSLAYSPGV AEPCLEIEKD QNKIYEYTNK
SNFVAVVTDG SAVLGLGNIG APASLPVMEG KAVLFKEFAG VDAFPICFNE SDPDKLISYV
KKIAPVFGGV NLEDIKSPEC FYIEDRLKEE LDIPVFHDDQ HGTAIITLAA LINSLILLKK
NIEDIKVIVN GAGAAGASII KLLHSEGVEE IIALDIKGAI YEGRDSLDES TKEIAKITNK
DNKKGDLAEM IKGADVFIGV SAANLLYKEM VRTMADDPII FAMANPEPEI WPEDALKAGA
KIVGTGRSDY PNQVNNVLAF PGLFRGALDV RAKEINEEMK KAAAYALANL IDENELAPDY
VIPKPFDPRV GPHVAAAVAQ AAVKTGVARI EIDYEAELEK AKNIMKKINK
//