ID A0A3B0BPB9_9BACL Unreviewed; 467 AA.
AC A0A3B0BPB9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:RKN74149.1};
GN ORFNames=D7M11_27240 {ECO:0000313|EMBL:RKN74149.1};
OS Paenibacillus ginsengarvi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN74149.1, ECO:0000313|Proteomes:UP000282311};
RN [1] {ECO:0000313|EMBL:RKN74149.1, ECO:0000313|Proteomes:UP000282311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN74149.1,
RC ECO:0000313|Proteomes:UP000282311};
RX PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA Yoon M.H., Ten L.N., Im W.T.;
RT "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT cultivation.";
RL Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN74149.1}.
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; RBAH01000025; RKN74149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0BPB9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000282311; 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; IPR002912; ACT_dom.
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; PS51671; ACT; 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:UP000282311}.
FT DOMAIN 7..80
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 467 AA; 50025 MW; 2A9E3009021E042F CRC64;
MAQTSIIIRL ELDHAQATFA DVASAISTAG GDITSIDVIR PGQDTSVRDI TVDVAESAET
EVVEALRRQE GIKLINVSDR TFLVHLGGKI AVQPNMPIRN RDDLSRVYTP GVAKVCTAIH
DNPNKVYSLT IKRNTVAVIS DGTAVLGLGD IGPHAAAPVM EGKAMLFKQL AGVDAFPICL
DTKDTEEIIR TIKAISPVFG GINLEDISSP RCFEIETRLA DELDIPVFHD DQHGTAVVLL
AGLLNALKVV GKRIDEVRVV VNGIGAAGVS VCKMLLAAGV RRLVPVDKDG AIVRGGTYGL
PMWSWLAEQP QVEATAGGLK DVLRGADVFI GVSRGGLLGA EDLQTMAPER IVFAMANPRP
EVDPEEALPF VRVLGTGRSD YPNQINNVLA FPGIFRGALD CRATRINEPM KLAAARAIAS
VVSESELSEQ YIIPSIFNEQ VVTKVRHAII EAAILTGTAR RTPPDFR
//
