ID A0A0F9XHK8_TRIHA Unreviewed; 669 AA.
AC A0A0F9XHK8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KKP04010.1};
GN ORFNames=THAR02_03861 {ECO:0000313|EMBL:KKP04010.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP04010.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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}.
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:KKP04010.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JOKZ01000090; KKP04010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XHK8; -.
DR OMA; QQAFMDE; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000034112; 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 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: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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112}.
FT DOMAIN 168..348
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 358..625
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 333
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 334
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 357
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 556
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 669 AA; 74140 MW; AF4F598AFD4C58DB CRC64;
MASSARSADS SDVFTPRSTS PSPSVASGRS SHRSSRTSVS NKRVSISSRR LTDFNPMSSV
DVLAIEEAMK LASLDQHRGY AQDHYTEVKQ DHDTEYLKES EASAYQVLRE PLWNKGLSFT
PEQRVAKNLT GLLPHAMESL ETQCARAMKM IHSRQTGIDK YLYLSSVKAQ NVDLFYRLLM
DNIRDLMPLV YTPTIGDVCL QYSTLYTRPE ALYISIKQRK SIRTMLRNWP CPNPEICVVT
DGSRILGLGD LGINGVGISI GKLALYTAAA GIHPAKTLPI VLDTGTNNET NLKDPFYLGL
RQKRVPFAEQ QAFMDEFMEA VKEVYPNMVV QFEDFDSEKA FNYLDRYRNN YRAFNDDIQG
TGAVVLAGYI NAVNLSSVPL EEQRLVFMGA GSAGVGVAKQ LVEYYTRRGL TEAEARDKFF
LVDTKGLVTM DRGDKLAEHK KYFARVDNAG HQFRTLEEVI EYVKPSALVG LAATFGIFTE
SVVRALKASV DAGGLGRRPI LFPLSNPLTK AECTFEQAVQ WTDGSVVFAS GSPFSSFTLK
VGGDAGDITY HPNQGNNVYV FPGLGLGAIL SKATRVTDEM VYTSAAALAG SLNAEEVHQG
LIYPKIDRVR DASIIVAREV MKAARRDGVS ELPESLWIEW EEWGDVALTN YIKQRVYNPT
SFSEAKGRL
//
