ID D9X491_STRVT Unreviewed; 572 AA.
AC D9X491;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EFL35919.1};
GN ORFNames=SSQG_06437 {ECO:0000313|EMBL:EFL35919.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35919.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG657757; EFL35919.1; -; Genomic_DNA.
DR AlphaFoldDB; D9X491; -.
DR STRING; 591159.SSQG_06437; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_11; -.
DR Proteomes; UP000004184; 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 Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT DOMAIN 87..269
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 279..540
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 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 254
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 255
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 572 AA; 61272 MW; F9279EAD3A935399 CRC64;
MRGVIMGTER STVDGVIRTS ARGHSVLNSP RLNRGTAFTR RERRELGLVG LVPPQVLTQD
QQAARAYAQF RSQPDDLAKN VYLTALRDRN EVLFHRLLGD HLAEMLPIVY TPTVGTAIER
YSYEYRRPRG VYLSVDDPDA IESSLRASGL GADDVDLIVA TDGEAILGIG DWGVGGIDIA
VGKLAVYTAA AGVDPARTLA VMLDVGTDRQ DLLDDPLYLG NRHPRVDRDR YDAFIDAYVT
AATKLFPDAL LHWEDFGSSN ARRVLDRYRE KTLTFNDDIQ GTGAVNLAAV LSGVRAGGAA
LRDHRVVLFG AGTAGVGIAE QLRDAMIADG LTSREAAGRI WAVDRHGLLT DGQQGLRDFQ
MPFARRRAEV ADWRHDEDLG GVPLAEVVDR VRPSVLIGTS GQGGAFTEDI VRSMAAHTDR
PVILPLSNPT RLAEAVPADL LAWTGGRALI ATGSPFAPVE TDGVTHHIGQ ANNALVFPGL
GLGTAVARAG RITDGMLVAA ARAIADQTDA TAPGAPILPP IDRLRDTSVA VAVAVARAAV
ADGVAREPVD DTVEERVRAA MWLPEYPPIE AV
//
