ID A0A0S8KCT9_9CHLR Unreviewed; 377 AA.
AC A0A0S8KCT9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KPL18877.1};
DE Flags: Fragment;
GN ORFNames=AMJ93_13465 {ECO:0000313|EMBL:KPL18877.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL18877.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL18877.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL18877.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL18877.1}.
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DR EMBL; LJUZ01000240; KPL18877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KCT9; -.
DR Proteomes; UP000052016; 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 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 26..159
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 173..377
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 47
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT NON_TER 377
FT /evidence="ECO:0000313|EMBL:KPL18877.1"
SQ SEQUENCE 377 AA; 40934 MW; 942ADDE9CE51DA70 CRC64;
MYNVDELLAK AKKPSEDALR LHPFYRGKVA TAAKCAVRDF QDFAIWYTPG VAAPCRAIAK
NPELVYEHTN KANVIAVVSD GTRVLGLGDI GPEAGLPVME GKALLFKYLG GVDAVPLCLD
TKDPDEIIRT VKLIQPSFGG INLEDISQPK CFRVLDTLRA DPEMTIPVWH DDQQGTATVL
LAGLINALKL VGKSMPEVKI TMVGFGAANV ATLRLLRASG ASMPNLVAVD SKGILHRDRK
DIEEKQNLFP DKWRICLESN AENRRGDAGE ALRGADVCIA FSKPGPGTIK PEWVRSMAKD
AIVFPCANPV PEIWLWEAKE AGARIVGTGR SDFANQLNNS LGFPGIFRGT LDVRARTITD
EMCLAAAQEL AQCAEDK
//
