ID A6GSV2_9BURK Unreviewed; 767 AA.
AC A6GSV2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:EDM82826.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:EDM82826.1};
GN ORFNames=LMED105_16233 {ECO:0000313|EMBL:EDM82826.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM82826.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM82826.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM82826.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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:EDM82826.1}.
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DR EMBL; ABCT01000013; EDM82826.1; -; Genomic_DNA.
DR AlphaFoldDB; A6GSV2; -.
DR STRING; 391597.LMED105_16233; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000010322; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) 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: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; 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 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EDM82826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010322}.
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 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 767 AA; 83618 MW; 9FABB30505A699B4 CRC64;
MDQRFRQAAL EYHEFPKPGK LQISATKSLV NQRDLALAYS PGVAAACEEI EADPSTAVRY
TAKANLVGVV TNGTAVLGLG NIGPLAAKPV MEGKAVLFKK FAGIDVFDIE INENDPDKLI
EIIASLEPTF GGINLEDIKA PDCFKVERAL RGRMNIPVFH DDQHGTAIVV GAAILNGLEV
IGKKLDEVKF VVSGAGAAAL ACLELLVELG LPRKNVWVTD IDGVVYKGRT TNMDPDKDLF
AQDTDARTLA DVIKDADVFL GLSAGGVLKQ DMVRAMAAKP LILALANPTP EILPEQVKEV
RDDAIMCTGR TDYPNQVNNV LCFPFIFRGA LDVGATTITK EMEIAAVRAV AELARKEQSD
VVASAYRTQN LSFGPEYLIP KPFDPRLIVH IAPAVAKAAM ESGVATRPIA DLEAYKDQLQ
QFVYHSGTFM KPIFAVAKRC VAETPQTSRI VFAEGEDERV MRAVQVVVDE AIAKPIMIGR
PAVIERRLER FGLRIKPGVD FELINPEYDE RYKDYWRMYH DLTKRKGVTE AYAKIEMRRR
NTLIGSMMIH KGNADGMICG TFGTHSLHLH YVDQVLGRRA GCNTYGAMNG LMLTNRQVFL
VDTHVNYDPT AEQIAEITLM AAEEMLRLGV QPKAALLSHS NFGSSNQPSA VKMREALQIL
RNIAPWLEVD GEMHGDCAID EQVRNTIFSG STLTGEANLL VCPNIDAANI SYNLLKSAAG
NGIAVGPILL GSDKPVHILT ASATVRRIVN MTALAVLDAN SERVSSL
//
