ID A0A0W0WWR4_9GAMM Unreviewed; 580 AA.
AC A0A0W0WWR4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KTD36771.1};
GN Name=sfcA_1 {ECO:0000313|EMBL:KTD36771.1};
GN ORFNames=Lnau_1755 {ECO:0000313|EMBL:KTD36771.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36771.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD36771.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36771.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KTD36771.1}.
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DR EMBL; LNYO01000013; KTD36771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0WWR4; -.
DR STRING; 45070.Lnau_1755; -.
DR PATRIC; fig|45070.6.peg.1840; -.
DR Proteomes; UP000054725; 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; 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 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,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 96..276
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 286..547
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 285
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 478
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 580 AA; 65230 MW; BD83FB98A991730A CRC64;
MSLYLIKKIM LDFKIIRDEQ TDELYIETSI CGKPLLTIPQ LNKSTAFTQE ERHEFGLLGK
LPHRVETLDE QVKRSYLQYS SYRTRMQQHI YLNNLHDKNQ VLFYKLLSRH LGEMLPIIYT
PIVGTAVKRF SHEYRQPRGL YIAHSDKNRI EEIISNRSNP EIDLIVVTDG EGVLGIGDQG
IGGMDIPVAK LMVYTLCGGI NPIRTLPVFL DVGTNNQELL NDPLYLGCQH PRIASEHYDD
FILSFVNAVR SHFPNAFLHW EDFGRSNARR ILDKFQNELC TFNDDIQGTG AVTLAALLSA
CDVTGINLED HRIVVFGAGS AGTGISDQIV DAMVRRGLKK EEAYQRFWLI DRQGLLVDSD
IELTEAQKPY ARKAKEISVW PILNKPFPSL TDTVRQIKPT ILIGCSAQPG AFSQEIIEIM
ASTSLRPVIF PLSNPDEKCE AQPADIMAWS QGKALIATGT AFPAVEYQNR LIEIAQCNNA
LVFPGVGLGI LAVQASRLSK EMIWAAAEAL SEYAPSKKDS YLPLLPSLDE AQIVAKHIAI
RVAKIAIKEG LAQKNQEANL DKLIQELFWE PRYLPFRKLK
//
