ID A0A0Q8R9U7_9BURK Unreviewed; 770 AA.
AC A0A0Q8R9U7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KRB92880.1};
GN ORFNames=ASE07_14730 {ECO:0000313|EMBL:KRB92880.1};
OS Noviherbaspirillum sp. Root189.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB92880.1, ECO:0000313|Proteomes:UP000051303};
RN [1] {ECO:0000313|EMBL:KRB92880.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB92880.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB92880.1, ECO:0000313|Proteomes:UP000051303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root189 {ECO:0000313|EMBL:KRB92880.1,
RC ECO:0000313|Proteomes:UP000051303};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRB92880.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMHZ01000006; KRB92880.1; -; Genomic_DNA.
DR RefSeq; WP_057289675.1; NZ_LMHZ01000006.1.
DR AlphaFoldDB; A0A0Q8R9U7; -.
DR STRING; 1736487.ASE07_14730; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000051303; 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; 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; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051303}.
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; 84083 MW; 58A8B5BF609F336D CRC64;
MESSTDQKEA LRQQLRQAAL EYHEFPTPGK ISVTPTKQLT NQRDLALAYS PGVAAACEEI
VIDPANAFKY TARGNLVAVI TNGTAVLGLG NIGPLASKPV MEGKGVLFKK FAGIDVFDIE
INETDPDKLC DIIAALEPTF GGVNLEDIKA PECFYIERKL RDRMKIPVFH DDQHGTAIIV
GAAILNGLKV VGKDIKNCKL VVSGAGAAAL ACLDLIVDLG FPIENIFVTD LAGVVYKGRT
ELMDPDKERF AQETSARTLS DVIPDADIFL GLSAGGVLKP EMVARMKARP LILALANPTP
EILPEEVKAV RNDAVIATGR SDYPNQVNNV LCFPYIFRGA LDCGATTITR EMEIAVVHAI
ADLAQAEQSD IVATAYGISN LSFGPEYLIP KPFDPRLMIK IAPAVAKAAE ESGVASRPIQ
DMQAYIDSLQ QFVYRSGTFM KPIFQIAKKA PAARKRIVFA EGEEERVLRA VQVVIDEKLA
QPILVGRPAV LAQRIEKFGL RMRPEVDFET INPEYDERYR EFWQEYLAMT RRKGVTEQYA
KLEMRRRHTL IGAMMIHKGA ADGMICGTFG TTALHLHYID QVLGKREGVN VYAAMNALIL
PDRQVAMVDT HVNENPTAEQ LAEITILAAE EMRRFGLLPR AALLSHSNFG TSNSESARKM
RAALEIIRER APDLEADGEM HGDTALDPVL LKTVMPDSPL KRDANLLVLP NIDAANISYN
LLKTAAGNGI AIGPILLGCS KPVHVLTPSA TVRRIVNMTA LCVMDAVAER
//
