ID W6JSZ1_9MICO Unreviewed; 392 AA.
AC W6JSZ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Malate oxidoreductase {ECO:0000313|EMBL:CCH71827.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:CCH71827.1};
GN ORFNames=BN11_1110004 {ECO:0000313|EMBL:CCH71827.1};
OS Tetrasphaera australiensis Ben110.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH71827.1, ECO:0000313|Proteomes:UP000035763};
RN [1] {ECO:0000313|EMBL:CCH71827.1, ECO:0000313|Proteomes:UP000035763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH71827.1,
RC ECO:0000313|Proteomes:UP000035763};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH71827.1}.
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DR EMBL; CAJA01000015; CCH71827.1; -; Genomic_DNA.
DR RefSeq; WP_048696692.1; NZ_HG764815.1.
DR AlphaFoldDB; W6JSZ1; -.
DR STRING; 1193182.BN11_1110004; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000035763; 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 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; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 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:0000313|EMBL:CCH71827.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035763}.
FT DOMAIN 29..162
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 174..390
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 392 AA; 40534 MW; F8D62B201D968272 CRC64;
MPTAEATARA QSEIPAELER DPVFVAHEGG KTAMVATKPL VDRDDLARLY TPGVAKVSSA
IAADPHLADA YTARRNTVAV VSDGTAVLGL GDIGPLAALP VMEGKAVLFK QFAGVDAVPL
CIETGSVDEI VDAVARLAPS FGGINLEDIS APRCFDIEER LGRRLGIPVF HDDQHGTAIV
VLAGLLNAAR VLSRDLSSMR MVISGAGAAG VAIAKLLIAV GVEDLIVCDS RGILCRGRVD
LTGHKLKLAR ATNPRRVQGS LADALAGADV FVGVSGGVVP ETDIATMALQ GIIFALANPN
PEVHPEVAGR YAGVVATGRS DYPNQINNVL AFPGIFRGAL DSGAADITEP MKLAAAHAIA
DLVDIPTPSE IVPCVFDVRV APAVAEAVAR HV
//
