ID I1YL68_METFJ Unreviewed; 561 AA.
AC I1YL68;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:AFJ03661.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:AFJ03661.1};
GN OrderedLocusNames=Q7C_2540 {ECO:0000313|EMBL:AFJ03661.1};
OS Methylophaga frappieri (strain ATCC BAA-2434 / DSM 25690 / JAM7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754477 {ECO:0000313|EMBL:AFJ03661.1, ECO:0000313|Proteomes:UP000009145};
RN [1] {ECO:0000313|EMBL:AFJ03661.1, ECO:0000313|Proteomes:UP000009145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM7 {ECO:0000313|EMBL:AFJ03661.1,
RC ECO:0000313|Proteomes:UP000009145};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003380; AFJ03661.1; -; Genomic_DNA.
DR RefSeq; WP_014705079.1; NC_017856.1.
DR AlphaFoldDB; I1YL68; -.
DR STRING; 754477.Q7C_2540; -.
DR KEGG; mec:Q7C_2540; -.
DR PATRIC; fig|754477.3.peg.2494; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000009145; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd05312; NAD_bind_1_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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFJ03661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009145}.
FT DOMAIN 79..259
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 269..527
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 244
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 268
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 561 AA; 61979 MW; 459B1FDFC5DDD951 CRC64;
MSAKSRRPIY LSYSGPQLLA TSLLNKGTAF SATERRDFNL DGLLPARFET LEEQAHRAYL
QYQSFAEPIN RHIYLRMVQD TNETLFYYLL NKHLAEMMPI IYTPTVGDAC ERFSEIYRRA
RGLFISYPDR DNLDAILHNA TKRHVKVIVV TDGSRILGLG DQGAGGMGIP IGKLSLYTVC
GGISPAYTLP ILLDVGTDNP ELLHDPHYIG WQHPRISDQQ YDAFVEKFIC ALQTRWPDAL
LQFEDFQQSK ALPLLQRYQN RLCCFNDDIQ GTAAVTVGTL LSACRIQNQP LSNQRIVFAG
AGSAGCGIAA QIIRQMQQEG LSEADAKKRI LLIDRQGLLS QAMSNLPDFQ LQLAASTDEL
DQLGLASGAD LLTVIQKAQP TVLIGVSGQR GLFSRTIIET MQDNCPQPII FPLSNPSKQI
EATPEEIMQW TQGKALIATG SPFAPVQIAQ QNYHIAQCNN SYIFPGIGLA VIIAGIKQIT
DNLMMTASNV LATAAANQTI DQGLLPPITA CQQISRDIAL AVAQQAIKDN LAPPQTLAML
EAALEKHFWQ PAYRSYRRTS D
//
