ID A0A1M5BD35_9BACL Unreviewed; 479 AA.
AC A0A1M5BD35;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:SHF40389.1};
GN ORFNames=SAMN05444392_12123 {ECO:0000313|EMBL:SHF40389.1};
OS Seinonella peptonophila.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Seinonella.
OX NCBI_TaxID=112248 {ECO:0000313|EMBL:SHF40389.1, ECO:0000313|Proteomes:UP000184476};
RN [1] {ECO:0000313|EMBL:SHF40389.1, ECO:0000313|Proteomes:UP000184476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44666 {ECO:0000313|EMBL:SHF40389.1,
RC ECO:0000313|Proteomes:UP000184476};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQVL01000021; SHF40389.1; -; Genomic_DNA.
DR RefSeq; WP_073158410.1; NZ_FQVL01000021.1.
DR AlphaFoldDB; A0A1M5BD35; -.
DR STRING; 112248.SAMN05444392_12123; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000184476; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184476}.
FT DOMAIN 99..232
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 244..466
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 120
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 218
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 479 AA; 52055 MW; 001FD516995AB8FE CRC64;
MNQQLYTNQP SIAGKSFILR LEMDTDQVQF ANVAKVIAEA GGDIIALDMI QTGSQMTVRD
ITVTVTKNDT IEQIEYHLKS LSGVRLLHIS DRTFLLHLGG KVEISPKIPI QNRDDLSRVY
TPDVARVCLA IQEQPEKAHT LTIKRNTVAV ISDGSAVLGL GNIGASAAMP VMEGKALLFK
QFAGIDAFPI CLDTQDTQQI IETIKAMAPT FGGINLEDIS SPRCFDIEKR LNEELDIPVF
HDDQHGTAVV LLAGLMNAMK VVGKPLDKIR VVVCGIGAAG LSCTKMLMAA GVKNIIGYDK
AGALTRDVQY DNPHWQWFAE NTNPERKTGT IGEVLEGADV FIGLSRGGVL KREDVMKMAS
QPVVFAMANP DPEIHPAEIE DIAAVIATGR SDYPNQINNV LCFPGIFRGA LDCRAETINE
EMKLAAAKAI ASVISDHERN PGYIIPSVFN QNVVQAIRTQ VVDAAIRTGV ARKIPSDFK
//
