ID F7VWQ7_SORMK Unreviewed; 859 AA.
AC F7VWQ7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=WGS project CABT00000000 data, contig 2.11 {ECO:0000313|EMBL:CCC09948.1};
GN ORFNames=SMAC_02528 {ECO:0000313|EMBL:CCC09948.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC09948.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC09948.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC09948.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC09948.1}.
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DR EMBL; CABT02000011; CCC09948.1; -; Genomic_DNA.
DR RefSeq; XP_003352093.1; XM_003352045.1.
DR AlphaFoldDB; F7VWQ7; -.
DR STRING; 771870.F7VWQ7; -.
DR GeneID; 10809785; -.
DR KEGG; smp:SMAC_02528; -.
DR VEuPathDB; FungiDB:SMAC_02528; -.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_2_1_1; -.
DR InParanoid; F7VWQ7; -.
DR OMA; QQAFMDE; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 372..552
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 562..823
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 68..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94896 MW; 73A1EC02A021DF1F CRC64;
MGKNRLPVSP WTVLMSGATA RLQKALSRPV LSSKLDGGRT SSHHLSSLTL TKSLLLASRF
AASTLVATTT STTSAGVSTS TGTSNPDPGT TIRSQTNRNP STYTSPPNSF SRKFSWGNLL
GWHQRTLPNK YKYNYGTHDP QGHLNPSSTT TRTTDTTLST SSHGERAESP YFNLTGHLDD
LSSLIRPFLA FLDPSSLSSS YSMASYAFST SSGSDLSTPR SSSPHSSASV ASARSSHSST
FSAAKRMSIS SVRRTSASNP MSSVDLSTIQ EALKMASLDT LRGYCQNTYG EVHQETATEY
IPHEEARGYQ VLNEPHWNKG TSFTPEERVS KNLTGLIPHV MEDSEKQVER ALKMIRTRQT
DIDRYLYLST IKSHNVDLFY RILMDHAKEM MPLVYTPTIG DVCLQYSTLY TRPEALYISI
KQRKSIRTIL RNWPYPKPEI CVVTDGSRIL GLGDLGVNGV GIPIGKLALY TAAAGIHPDK
TLPIVLDCGT ANETNLRDPL YLGLRQKRIP VSEQQEFMDE FMEAAAEVFP EMVVQFEDFE
SEKAFNYLDR YRDQYKCFND DIQGTGAVVL AGYIGAVNLS NVPIEEQRLV FMGAGSAGVG
VAKQLVEYYT KRGLSEQQAK DKFWLVDTKG LVTKDRGDKL AEHKKYFART DNNGHQFRTL
EEVIEYVKPS ALVGLTATHG VFTESVVRAL KASVDAGGLG RRPILFPLSN PLTKAECTFK
EAVDWTEGTV LFASGSPFSN YTVNGVTYHP NQGNNVYVFP GIGLGAILAK ASKVTDDMIY
TSAAALSNSL NADEVKQGLI YPRIDRVREA SVIVAREVMK SARREGVSTL PEEQWLEWEE
WGDVALDRYI KQHVYDPML
//
