MAO1_PSEU2
ID MAO1_PSEU2 Reviewed; 563 AA.
AC Q4ZW63;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NAD-dependent malic enzyme {ECO:0000255|HAMAP-Rule:MF_01619};
DE Short=NAD-ME {ECO:0000255|HAMAP-Rule:MF_01619};
DE EC=1.1.1.38 {ECO:0000255|HAMAP-Rule:MF_01619};
GN Name=maeA {ECO:0000255|HAMAP-Rule:MF_01619}; OrderedLocusNames=Psyr_1561;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=1.1.1.38; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01619};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01619};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000255|HAMAP-Rule:MF_01619};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01619}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000255|HAMAP-
CC Rule:MF_01619}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY36609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000075; AAY36609.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003317398.1; NC_007005.1.
DR RefSeq; YP_234647.2; NC_007005.1.
DR AlphaFoldDB; Q4ZW63; -.
DR SMR; Q4ZW63; -.
DR STRING; 205918.Psyr_1561; -.
DR EnsemblBacteria; AAY36609; AAY36609; Psyr_1561.
DR KEGG; psb:Psyr_1561; -.
DR PATRIC; fig|205918.7.peg.1595; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_6; -.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR Gene3D; 3.40.50.10380; -; 1.
DR HAMAP; MF_01619; NAD_malic_enz; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR023667; NAD_malic_enz_proteobac.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..563
FT /note="NAD-dependent malic enzyme"
FT /id="PRO_0000160226"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 244
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 267
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT BINDING 416
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
FT SITE 267
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01619"
SQ SEQUENCE 563 AA; 62285 MW; C4D76794E57CB6EA CRC64;
MTKTSRPLYI SYAGPSLLEM PLLNKGSAFT PQERVEFNLI GLLPQNVETI EEQVTRVYSQ
YKQCASDLDK HIYLRSIQDN NETLFFRLLD SHLDEMLPII YTPTVGQACQ EFSKIYRTHR
GLFISYPERD RIDDILRSAT KDRIKIIVVT DSERILGLGD QGIGGMGIPI GKLSLYTACG
GISPAYTLPI VLDVGTNNRE LLDDPMYMGW RHERVSGKEY EDFIALFIDA VQRRWPDVLL
QFEDFAQSNA MPLLEKYRDE LCCFNDDIQG TASVAVGTLL AACKAKNETL GQQKVVFVGA
GSAGCGIAEH IIAAMRIEGL SESEARKRIF MVDRFGLLTE SMDNLLDFQK RLAQKTADVS
GWTAGSEAFP QLLDVVTHAG ATVMIGVSGQ RGLFTEQVIR ELHKHCAKPL VMPLSNPTSK
VEATPEEILR WTDGNALVAT GSPFAPVEIN GRTVHIAQCN NSYIFPGIGL GVVACKASRI
TDRMLMAASN ALAECSPMVT GKGDAVLPPL KEIQQVSRKI ALAVAREAQA EGLALETTEE
ALLEAIERNF WLPGYRAYRR RSV
