ID K2C0X6_9BACT Unreviewed; 298 AA.
AC K2C0X6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Malic enzyme NAD-binding domain-containing protein {ECO:0000259|SMART:SM00919};
DE Flags: Fragment;
GN ORFNames=ACD_44C00333G0001 {ECO:0000313|EMBL:EKD74778.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD74778.1};
RN [1] {ECO:0000313|EMBL:EKD74778.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {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:EKD74778.1}.
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DR EMBL; AMFJ01018516; EKD74778.1; -; Genomic_DNA.
DR AlphaFoldDB; K2C0X6; -.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU003427}.
FT DOMAIN 1..262
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD74778.1"
SQ SEQUENCE 298 AA; 32240 MW; A228FFD667BF8648 CRC64;
IQGTAAIAVG TILAALHITK MSLSQQRIVI FGAGGAGCGI AKLFVSTLIA QGVKEKEAYR
SVYLIDRSGL MMEGVPHALP FQIPFLKPRA MIENWKLKDP SKISLLDTIL NAKPSILLGV
SGQGGVFTEE IIKAMAAHVE NPIIFPLSNP TSNSEAIPQD LMTWTNDKAI ISTGSPFGNI
FKNKEAFHVD QTNNSYIFPG IGLGLIASQS TRATDNMFMI AAKILADCSP AKTNPKANLL
PKIPKIREVS YKIGLAVAKE AVAQGLSLLP AHEQENLENR VKETMWTPEY LPYVLTKT
//