ID A0A158DKS0_9BURK Unreviewed; 758 AA.
AC A0A158DKS0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:SAK95115.1};
GN ORFNames=AWB79_07189 {ECO:0000313|EMBL:SAK95115.1};
OS Caballeronia hypogeia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777140 {ECO:0000313|EMBL:SAK95115.1, ECO:0000313|Proteomes:UP000054851};
RN [1] {ECO:0000313|Proteomes:UP000054851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; FCOA02000048; SAK95115.1; -; Genomic_DNA.
DR RefSeq; WP_061172194.1; NZ_FCOA02000048.1.
DR AlphaFoldDB; A0A158DKS0; -.
DR STRING; 1777140.AWB79_07189; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000054851; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
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 Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 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; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2,
KW ECO:0000256|RuleBase:RU003427};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 758 AA; 81331 MW; 69B599F6A36ADF0A CRC64;
MDEQLKQSAL AYHQNPRPGK ISVTPTKPLS NQLDLSLAYS PGVAAACMAI YDEPLDAQKY
TSRANLVGVV TNGTAVLGLG NIGPLAAKPV MEGKGCLFKK FAGIDVFDIE LAETDPDKLV
EAIAMLEPTL GGINLEDIKA PECFYIEKKL RERMKIPVFH DDQHGTAIIA SAAILNGLKV
VGKKLDEVKL VCSGAGAAAI ACLDLLVHLG LKKSNTLVID SKGVIYEGRG NLDASKERYQ
ASTDARTLAD AMHGCDVFLG CSSAGVLKAE MVQTMADKPL ILALANPEPE IRPEEAKRVR
PDCIVATGRS DYPNQVNNVL CFPFIFRGAL DVGATTITEE MKLACVRAIA ELAEETDQGD
EVAKAYEGHS LEFGPEYLIP KPFDPRLIIK IAPAVAQAAM DSGVATRPIK DMDAYRETLG
ATVYRTGMVM RPVFATAKSA PARIAFAEGE DERVLRAAQF VLLEKIAKPI IIGRPAVVEM
RLQKMGSKLK PGVDFEIVNP EDDPRYQKSW QAYHEIAARQ GVTPEGAKAA LRKFNTLIGA
ILVHTGDADG MICGLIDTYQ DHLKFIEQVL GKAPGVKNFA AMNLLMLQGR NLFISDTYVN
ETPTPEQLAD MTILAAREIE RFGVQPKVAL LSNSNFGSVA SASSQRMAEA RKLIAERAPN
LEIDGEMHGD AALSEAVRKA AFPGTTLHGE ANLLIMPNVE AANITYNLLK MVSGEGVTVG
PFLLGAAKPV HILTPAATVR RIINMTAVAS AGAAVGNK
//
