ID A0A1V9USB2_9PSED Unreviewed; 562 AA.
AC A0A1V9USB2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD-dependent malic enzyme {ECO:0000256|HAMAP-Rule:MF_01619};
DE Short=NAD-ME {ECO:0000256|HAMAP-Rule:MF_01619};
DE EC=1.1.1.38 {ECO:0000256|HAMAP-Rule:MF_01619};
GN Name=maeA {ECO:0000256|HAMAP-Rule:MF_01619};
GN ORFNames=BWR59_12570 {ECO:0000313|EMBL:OQR32782.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR32782.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR32782.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR32782.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01619};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01619}.
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|HAMAP-Rule:MF_01619,
CC ECO:0000256|RuleBase:RU003427}.
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:OQR32782.1}.
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DR EMBL; MUIN01000006; OQR32782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9USB2; -.
DR STRING; 1943632.BWR59_12570; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000192462; Unassembled WGS sequence.
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 GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd05312; NAD_bind_1_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 HAMAP; MF_01619; NAD_malic_enz; 1.
DR InterPro; IPR046346; Aminoacid_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 PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01619};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01619};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01619}.
FT DOMAIN 78..258
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 268..528
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 244
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 267
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 415
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT SITE 267
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
SQ SEQUENCE 562 AA; 62088 MW; 225EB4106783FE5B CRC64;
MTKTSRPLYI SYAGPSLLEM PLLNKGSAFT PQERVDFNLI GLLPQNVETI EEQVTRVYDQ
YKQCASDLDK HIYLRSIQDN NETLFFRLLD SHLEEMLPII YTPTVGQACQ EFSKIYRTHR
GLFISYPDRD RIEDILRSAT KDRIKIIVVT DSERILGLGD QGIGGMGIPI GKLSLYTACG
GVSPAYTLPI VLDVGTNNKE LLDDPMYMGW RHERVTGKEY EDFIALFIEA VQRRWPDVLL
QFEDFAQTNA MPLLEKYRDE LCCFNDDIQG TASVAVGTLL AACKAKNETL GQQRVVFLGA
GSAGCGIAEH IIAAMVIEGL SETEARKRVM MVDRFGLLTD SMDNLLDFQK NLAQKAGDVA
GWSSGEGYPE LLDVVSNGKP TVLIGVSGQR GLFTEQIIRE MHKHCAKPLV MPLSNPTSKV
EVTPQEVLTW TNGDALVATG SPFAPVTVGD RTFHIAQCNN SYIFPGIGLG VIAAKATRIT
DKMLMAASNA LAECSPMVTG KGDAVLPPLK EIQTVSKKIA LAVAKQAQEE GVALETTEEM
LVEAIERNFW MPNYRSYRRS AV
//
