ID A0A157SDN3_9BORD Unreviewed; 764 AA.
AC A0A157SDN3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:SAI68361.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:SAI68361.1};
GN Name=maeB_1 {ECO:0000313|EMBL:SAI68361.1};
GN ORFNames=SAMEA3906487_01212 {ECO:0000313|EMBL:SAI68361.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI68361.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI68361.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI68361.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-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: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; LT546645; SAI68361.1; -; Genomic_DNA.
DR RefSeq; WP_063491688.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157SDN3; -.
DR STRING; 123899.SAMEA3906487_01212; -.
DR GeneID; 56591496; -.
DR KEGG; btrm:SAMEA390648701212; -.
DR PATRIC; fig|123899.6.peg.1188; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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:SAI68361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..402
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 764 AA; 82620 MW; ECACCABF928446A6 CRC64;
MPQNPNHRQA ALDYHEFPRP GKIAITASKP LVTQRDLGLA YTPGVAAACE EIVTDPLNAF
RFTARGNLVG VISNGTAVLG LGNIGALASK PVMEGKAVLF KKFAGLDVFD IEINETDPDK
LVDIIAGLEP TFGGINLEDI KAPECFIVER KLRERMRIPV FHDDQHGTAI TVCAAFINGL
KVVGKDISQV KVVTSGAGAA ALACLDLMVD LGLPLQNIWA TDIEGVVYEG RTVLMDPSKA
RFAQPTEART LAEVIEGADV FLGLSAGGVL KPEMVAAMAA RPLILALANP TPEILPEDAH
AVRDDIVMAT GRSDYPNQVN NVLCFPYIFR GALDVGATTI TREMEKAAVY AIAALAQEEQ
NEVVAAAYGT YDLAFGPEYL IPKPFDPRLI ERIAPAVAQA AMADGVATRP IADIEAYVEQ
LQQFVYHSGA FMKPLFASAK RFVREGGRAR IVFTEGEDER VLRAVQVVVD EGLAKPILVG
RPAVLAARIE KYGLRLRLGQ DVEVTNPEYD ERFHQYWTTY WELMCRRGIT KEMARVEMRR
RMTLIGAMMV RLGDADGMVC GSVGAYHDHL RFVDEVIGKR PGAKTYAAMN ILLLDQRMVA
LVDTHVNDDP SAEQIAEFTI AAAEEMKRLN LAPKAALLSR SNFGTGSSAS GAKMREALEL
VRAQAPELEI DGEMHGDCAL DEALRLRILP SSSLKGEANL LVCPNVDAGN IAYNLLKTTA
GSNVAIGPFL LGPNAPVNIL TSSSSVRRII NMTALTVINA NRPA
//
