ID T0I6Y6_9FIRM Unreviewed; 418 AA.
AC T0I6Y6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:EQB21471.1};
GN ORFNames=UNSWDHB_1193 {ECO:0000313|EMBL:EQB21471.1};
OS Dehalobacter sp. UNSWDHB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1339256 {ECO:0000313|EMBL:EQB21471.1, ECO:0000313|Proteomes:UP000015814};
RN [1] {ECO:0000313|EMBL:EQB21471.1, ECO:0000313|Proteomes:UP000015814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNSWDHB {ECO:0000313|EMBL:EQB21471.1,
RC ECO:0000313|Proteomes:UP000015814};
RX PubMed=24051315;
RA Deshpande N.P., Wong Y.K., Manefield M., Wilkins M.R., Lee M.;
RT "Genome Sequence of Dehalobacter UNSWDHB, a Chloroform-Dechlorinating
RT Bacterium.";
RL Genome Announc. 1:e00720-13(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 -!- 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}.
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:EQB21471.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AUUR01000112; EQB21471.1; -; Genomic_DNA.
DR RefSeq; WP_015042406.1; NZ_AUUR01000112.1.
DR AlphaFoldDB; T0I6Y6; -.
DR PATRIC; fig|1339256.3.peg.1381; -.
DR Proteomes; UP000015814; 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; 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}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 166..391
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 418 AA; 44580 MW; FE8B04E01B9A0D13 CRC64;
MSRIKNLREE ALAFHAVRPG KLEVKVTVSA NDRDDLTLAY SPGVAEPVKE IAKDLANLDV
YTNHANYVCI VSDGTAILGL GNLGPAAAMP VMEGKALLFK AFADVDAFPI CVNTNDIDKI
VELVELIAPT FGGVNLEDIK APECFEIEGK LKARNIFKGP IFHDDQHGTA VVTLAGLFNA
LKVVGKSIDE IKVVTNGAGA AGIAIIKLMM SMGLKNVIMC DTKGAIYKGR PEGMNKYKDE
IAEKTNYEMC RGSLRDAIKG ADVFIGVSAP DSIDEEMIKS MAKDPIVFAQ ANPIPEIWPI
ERALDAGAAV ISTGRSDVIN QINNVLAFPG MFRGAIDVRA TDINDAMKIA AAQAIANCVK
PEELCADYII PSAFNPEVAA AVAAATARAA IESGIARNPI DPALVAENLK KRLANQYK
//
