ID B5Y841_COPPD Unreviewed; 399 AA.
AC B5Y841;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Malate oxidoreductase {ECO:0000313|EMBL:ACI17927.1};
GN OrderedLocusNames=COPRO5265_0583 {ECO:0000313|EMBL:ACI17927.1};
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI17927.1, ECO:0000313|Proteomes:UP000001732};
RN [1] {ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI17927.1, ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RX PubMed=24831154;
RA Alexiev A., Coil D.A., Badger J.H., Enticknap J., Ward N., Robb F.T.,
RA Eisen J.A.;
RT "Complete Genome Sequence of Coprothermobacter proteolyticus DSM 5265.";
RL Genome Announc. 2:e00470-14(2014).
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}.
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DR EMBL; CP001145; ACI17927.1; -; Genomic_DNA.
DR RefSeq; WP_012544578.1; NC_011295.1.
DR AlphaFoldDB; B5Y841; -.
DR STRING; 309798.COPRO5265_0583; -.
DR KEGG; cpo:COPRO5265_0583; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000001732; Chromosome.
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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001732}.
FT DOMAIN 13..144
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 156..376
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 399 AA; 43707 MW; 737F32848BD94D91 CRC64;
MEITPSFLHK LYRGKWELRV RVPLARNLHV FYTPGVAEPC QSIAADSALV WDMTNRWNTI
GVISNGTRIL GLGNIGPEAG LPVMEGKAVL YKYYAGIDAI PLCIRAETEE AILAFLSAIE
PSLGGINLED IKQPDAFNVL TEARKFLRIP IIHDDMEGTG IIMLAAVLAS SSMAGLKLES
EKIVLLGAGS ANMGFLQLLD ELLLGNIGNV IVVDRDLVYN SENSQQHWMG NILSKTNKLG
SSNLEEALKG ASFLIAASRP GPGVFPLEYL RNMKKPNTVL SLANPVPEVS REEACAMGVT
IYGSGRSDDP NQVNNSLIFP GLMLGLLVTQ QQYNTAVGIE VAKALSELAM KKQRIVPQMD
SEVHQFVART VVEHFSKKCA SKENASMWAE ELNWRMNRK
//
