ID A0A1I4GJI8_9FIRM Unreviewed; 406 AA.
AC A0A1I4GJI8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:SFL29497.1};
GN ORFNames=SAMN02983006_00767 {ECO:0000313|EMBL:SFL29497.1};
OS Halanaerobium salsuginis.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL29497.1, ECO:0000313|Proteomes:UP000199006};
RN [1] {ECO:0000313|EMBL:SFL29497.1, ECO:0000313|Proteomes:UP000199006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL29497.1,
RC ECO:0000313|Proteomes:UP000199006};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- 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}.
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DR EMBL; FOTI01000006; SFL29497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4GJI8; -.
DR STRING; 29563.SAMN02983006_00767; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000199006; 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; 2.
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:UP000199006}.
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 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 406 AA; 43451 MW; 780ED06A8AFADA2A CRC64;
MNIYQRALQL HQAKQGKLAV KSKVAVTNKE ELSLAYSPGV AEPCRAIQKN PENIYLYTAK
ANQVAVVSSG TAVLGLGDIG PEAALPVMEG KAVLFKEFAN VDAFPLCVGS KNIEKIVEFV
KLLEPTFAGV NLEDISAPEC FAIENRLKQE TNMAIFHDDQ HGTAIVVLAA VLNALELVEK
KLDQIKIVIN GAGAAATAVT KLLFDAGAQN IIINDKIGIL NSQNKVQFDS LRQQVIAQTN
RQDIAGGLAE AVAGADLFIG LSVADVLTKK MVETMAKQPL IFAMANPEPE IKPEIALQAG
AEVIATGRSD YPNQINNVLA FPGVFRGALD VRARAISEKM KIAAARAIAE LAASKLNSDY
IIPDPFDQRV VPTVALAVAR TAIKEGLARL ELTDNELKAK IKANLL
//
