ID A0A1R0YR89_9BACL Unreviewed; 472 AA.
AC A0A1R0YR89;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OME08789.1};
GN ORFNames=BSK60_28975 {ECO:0000313|EMBL:OME08789.1}, BSO21_19140
GN {ECO:0000313|EMBL:OMD29493.1};
OS Paenibacillus odorifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=189426 {ECO:0000313|EMBL:OME08789.1, ECO:0000313|Proteomes:UP000187446};
RN [1] {ECO:0000313|EMBL:OME08789.1, ECO:0000313|Proteomes:UP000187446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL F4-0242 {ECO:0000313|EMBL:OME08789.1,
RC ECO:0000313|Proteomes:UP000187446}, and FSL H7-0433
RC {ECO:0000313|EMBL:OMD29493.1, ECO:0000313|Proteomes:UP000187158};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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:OME08789.1}.
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DR EMBL; MPVP01000130; OMD29493.1; -; Genomic_DNA.
DR EMBL; MPTN01000041; OME08789.1; -; Genomic_DNA.
DR RefSeq; WP_076130640.1; NZ_MPVP01000130.1.
DR AlphaFoldDB; A0A1R0YR89; -.
DR STRING; 189426.PODO_11315; -.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000187158; Unassembled WGS sequence.
DR Proteomes; UP000187446; 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; 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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427}.
FT DOMAIN 88..221
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 233..455
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 472 AA; 50455 MW; A46D76F348FF063F CRC64;
MSIATTMIIR LEIRKSVASF GDVASGIAAA GGDIVAIDVI RAGKDVTTRD ITVNVQDAAN
GDIISILSKM PGIKIINVSD RTFLAHLGGK IEITPKMPIK NREDLSLVYT PGVARVCTAI
AEDPRKAYSL TMKRNTVAVV SDGTAVLGLG DIGPEAAMPV MEGKAMLFKQ LANIDAFPLC
LNTKDPDEII NIVKAVSPGF GGINLEDISS PRCFEIERRL AEELDIPVFH DDQHGTSVVA
FAGLLNALKV VNKSIENARI VVVGIGAAGV SICNLLLAAG ARYIYAVDRE GVLRKDLQYD
NPEWQKLAAA TNPEGIEGGI TEVIRGADVF IGVSRGGILT VDHLKSMASD NIVFAMANPT
PEIEPDLAEP FVRVLATGRS DYPNQINNVL CFPGIFRGAL DCRARTVNLE MKLAAAKAIA
SVVHPDELNE QYIIPSIFNE KVVEQVRLAV IQAAISTDAA RRIPKDVAAI TE
//
