ID A0A3P4AXG4_9BURK Unreviewed; 421 AA.
AC A0A3P4AXG4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:VCU68462.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:VCU68462.1};
GN Name=maeB_1 {ECO:0000313|EMBL:VCU68462.1};
GN ORFNames=PIGHUM_00513 {ECO:0000313|EMBL:VCU68462.1};
OS Pigmentiphaga humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2478468 {ECO:0000313|EMBL:VCU68462.1, ECO:0000313|Proteomes:UP000277294};
RN [1] {ECO:0000313|EMBL:VCU68462.1, ECO:0000313|Proteomes:UP000277294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DnA1 {ECO:0000313|EMBL:VCU68462.1};
RA Criscuolo A.;
RL Submitted (OCT-2018) 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}.
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DR EMBL; UWPJ01000005; VCU68462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P4AXG4; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000277294; Unassembled WGS sequence.
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 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; 2.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:VCU68462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277294}.
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 39
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 421 AA; 44966 MW; 17AF2AC7BAD35A3B CRC64;
MDASLVDQAL AYHQSPVPGK IAVVPTKPLD NQDDLSLAYS PGVAAACEAI ANEQQSVRLY
TSRSNLVAVI SNGTAVLGLG NIGPYAAKPV MEGKACLFQK FAGINVFDLE LAENDPDKLV
DAIAMMEPTF GGINLEDIKA PECFYIERKL TERMSIPVFH DDQHGTAIVA SAGIVNGLKL
AEKTIDQVKL VCSGAGAAAI ACLDLLVRQG MKKENILLVD SKGVVFEGRD ASMEFNKSRY
ATTGTARSLA DAVKDSDVFL GCSAAGLLTP EMVATMALRP LILALANPEP EIRPELAKAV
RSDAIIATGR SDYPNQVNNV LCFPFLFRGA LDVDAMRITD EMKLACVNAL AELARKPVHP
EAAKAHPNRK LEFGPDYIIP TPFDPRLISE LASAVALAAM DSGVARRPIS DIDAYRASLT
K
//
