ID A0A0W0V821_9GAMM Unreviewed; 575 AA.
AC A0A0W0V821;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Malate oxidoreductase {ECO:0000313|EMBL:KTD16223.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:KTD16223.1};
GN Name=sfcA_1 {ECO:0000313|EMBL:KTD16223.1};
GN ORFNames=Ljor_0529 {ECO:0000313|EMBL:KTD16223.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD16223.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD16223.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD16223.1,
RC ECO:0000313|Proteomes:UP000055035};
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:KTD16223.1}.
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DR EMBL; LNYJ01000011; KTD16223.1; -; Genomic_DNA.
DR RefSeq; WP_058470095.1; NZ_RDQP01000002.1.
DR AlphaFoldDB; A0A0W0V821; -.
DR STRING; 456.Ljor_0529; -.
DR PATRIC; fig|456.5.peg.559; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000055035; Unassembled WGS sequence.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
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-EC.
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,
KW ECO:0000313|EMBL:KTD16223.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055035}.
FT DOMAIN 87..267
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 277..538
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 252
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 253
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 575 AA; 64482 MW; 41E32E77AA8B150A CRC64;
MLDFKVIRDE QTGELVMETS ICGKPLLTTP QLNKSTAFTR EERQEFGLMG KLPHRVETLD
EQVKRAYLQY SSYSNRLQQN IYLNNLHDKN QVLFFKLISK HLGEMLPTIY TPIVGTAVKR
YSHEYRQPRG LYIAHSEKNY IEEIINNRSN PEIDLIVVTD GEGVLGIGDQ GIGGMDIPVA
KLMVYTLCGG LDPTRTLPVF LDVGTNNQDL LNDPLYLGCQ HPRIPVEDYD DFILTFVNAI
HKHFPNAFLH WEDFGRSNAR RILDKFQDKL CTFNDDIQGT GAVTLAALLA ACDVTGIELE
NHRIVVYGAG SAGTGISDQI VDAMVRRGHS PEEAYSRFWL IDRQGLLVNS DLELTEAQKP
YARKPEEIES WYSNSRHYPS LTDTVRQIRP TILIGCSAQP GAFSQDIIEI MSSTCERPIV
FPLSNPDDRC EAQPADIMTW SEGRALIATG TAFPAVEYQN RLLQIAQCNN ALVFPGIGLG
VLAVKALRLS KGMIWAAAEA LSEFAPSKKD SFLPLLPSLD DAQVVAKHIA VTVARKAIEE
NLAQINQDAD LETIIKDMFW EPRYLPFRKI KTKPA
//
