ID A2RPS6_HERSE Unreviewed; 770 AA.
AC A2RPS6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=NADP-dependent malic enzyme oxidoreductase protein {ECO:0000313|EMBL:CAM32583.1};
GN Name=maeB {ECO:0000313|EMBL:CAM32583.1};
OS Herbaspirillum seropedicae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=964 {ECO:0000313|EMBL:CAM32583.1};
RN [1] {ECO:0000313|EMBL:CAM32583.1}
RP NUCLEOTIDE SEQUENCE.
RA Chaves D.F.S., Ferrer P.P., Monteiro R.A., Souza E.M., Cruz L.M.,
RA Pedrosa F.O.;
RT "A two-dimensional proteome reference map of Herbaspirillum seropedicae
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAM32583.1}
RP NUCLEOTIDE SEQUENCE.
RG Genopar Consortium;
RA Pedrosa F.O.;
RT "Genome sequence of the nitrogen fixing bacterium Herbaspirillum
RT seropedicae.";
RL Submitted (FEB-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}.
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DR EMBL; AM490488; CAM32583.1; -; Genomic_DNA.
DR RefSeq; WP_013235305.1; NZ_JWZZ01000004.1.
DR AlphaFoldDB; A2RPS6; -.
DR KEGG; hsz:ACP92_16825; -.
DR PATRIC; fig|964.11.peg.3530; -.
DR OMA; NIWVTDL; -.
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; IPR032683; Malate_DH.
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; PF12434; Malate_DH; 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}.
FT DOMAIN 28..161
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 173..410
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 86..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 297
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 770 AA; 84231 MW; AB7B9ED98AEFF5D8 CRC64;
MDSMISKKEE VRQQLRQAAL DYHEFPTPGK IAVTPTKLLT NQRDLSLAYS PGVAAACEEI
VADPLNAFRY TARGNLVAVI SNGTAVLGLG NIGALASKPV MEGKGVLFKK FAGIDVFDIE
VNETDPDKLI DVIAALEPTF GGINLEDIKA PECFYIERKL REKMKIPVFH DDQHGTAIIV
GAAILNGLKV VGKDIKNVKL VVSGAGAAAL ACLDLIVDLG FPIENIYVTD LAGVVYKGRK
ELMDPDKERF ARETEARTLA EVIPDADIFL GLSAAGVLKP EMVKQMAARP LVLALANPTP
EILPEEVKAV RDDAIIATGR SDYPNQVNNV LCFPYIFRGA LDSGATTITR EMEIATVHAI
AELAQAEQSD IVATTYGIAN LSFGPEYIIP KPFDPRLMIK IAPAVARAAE SSGVAARPIQ
DMDAYIEKLE QFVYHSGTFM RPIFQVAKKA AEAKKRIVYA EGEEERVLRA VQVIVDENLA
KPILVGRPEV LEQRIQKFGL RLRAGTDFEV INPNFDNRYR DYWQTFLEMS RRKGVTEQYA
KLEMRRRHTL IGSMAIHKGD ADGMICGTYG TTQLHLHYID QVLGKREGVN VYAAMNAVIL
PNRQLVMVDT HVNENPNARE LAEITMLAAE EMRRFGLHPR AALLSHSNFG SSNSESARKM
REALAILREI APELEVDGEM HGDTALDSKL LNAVIPDSPL KGDANLLVMP NIDAANIAYN
LLKTASGNGV AIGPILLGCA KPVHILTPSA TVRRIINMTA LCVMDALSER
//
