ID A0A149Q5F2_9PROT Unreviewed; 544 AA.
AC A0A149Q5F2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KXU92568.1};
GN ORFNames=AD928_10905 {ECO:0000313|EMBL:KXU92568.1};
OS Acetobacter cerevisiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU92568.1, ECO:0000313|Proteomes:UP000075473};
RN [1] {ECO:0000313|EMBL:KXU92568.1, ECO:0000313|Proteomes:UP000075473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU92568.1,
RC ECO:0000313|Proteomes:UP000075473};
RA Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT "Improved classification and identification of acetic acid bacteria using
RT matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT respectively.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, 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:KXU92568.1}.
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DR EMBL; LHZA01000153; KXU92568.1; -; Genomic_DNA.
DR RefSeq; WP_062250503.1; NZ_LHZA01000153.1.
DR AlphaFoldDB; A0A149Q5F2; -.
DR PATRIC; fig|178900.5.peg.939; -.
DR Proteomes; UP000075473; Unassembled WGS sequence.
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: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 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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000075473}.
FT DOMAIN 75..255
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 265..516
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 544 AA; 60554 MW; 97D7A69887C2743B CRC64;
MPKAPIPHLR GMSLLNDASQ NKGTAFTAEE RRQYGLEGLL PTHVESLDRQ VERIHRHLEA
KPSDLERYIY LSGLRDQNET LFYRVLMSNP AKYVPIIYAP TLAAVCQQFS HIYRRPRGMY
ISLEMKGRIE EVLRNWPVDD VRVICVTTGG RILGLGDIGV NGMGIPIGKL HLYTACGAVP
PEPLLPIQLD IGTTNSALRA DPLYLGLRRE PPSQDVLDEF VEEFVQAVQT VFPRCCLHFE
DWKGTDAIRY LEKYYPRVRC YNDDIQGTAA VTLAGLITAL RIKNEPLTDQ RVLFLGAGSS
GLGIANMLVT AMQKEGMSEA EAVSRMTLMD VDGLLEKSRT DLSPQQARYA RDMPPSRDLL
AMVKAVKPTI LIGVSTCGGA FTQEVVEEMA ALNERPIIFA LSLPAKNGEC TAEQAYTWSE
GRALFAAGLQ YPEFTLNDKT FYPGQANNFY IFPALGLAVY ATCPDLITDD MVIKAAKALA
DQVDPAAQER GRLFPPQSEI LEVSITSATR IAEFIFDQGA ATMERPQDIR AWIESLIYTP
RYEH
//
