ID F9ZLY1_ACICS Unreviewed; 426 AA.
AC F9ZLY1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AEK57463.1};
GN OrderedLocusNames=Atc_0814 {ECO:0000313|EMBL:AEK57463.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK57463.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK57463.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK57463.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP002573; AEK57463.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZLY1; -.
DR STRING; 990288.Atc_0814; -.
DR KEGG; acu:Atc_0814; -.
DR HOGENOM; CLU_034446_2_1_6; -.
DR OrthoDB; 5287223at2; -.
DR Proteomes; UP000006135; Chromosome.
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 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; 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 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135}.
FT DOMAIN 38..171
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 183..419
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 426 AA; 45075 MW; 186CB41BBB0DCB34 CRC64;
MADAKSARSP DIGGGAADAQ RAEALRSRAL AYHAAAPAGK LAIEVTKPCT TQAQLSLAYT
PGVAAPVREI ARDPEFAYDY TAKGNLVAVV TNGTAVLGLG RVGPLAGKPV MEGKAVLFKH
FAGIDAFDIE VEARDADHLI DVVTAIAPGF GGINLEDIAA PDCFRVEREL QERLDIPVFH
DDQHGTAVIV AAALRNALIV QEKNLESVKV AIVGAGAAGV AIARMLQSMG VQRCFLSDVH
GVLHRGRKDL SPWHDDLAVA PEDWTLAEML ADADVVIGVA VRGAIPEAAL PTLAPRPVVF
ALANPDPEID PRRVRQLRPD AVIATGRSDL PNQVNNALGF PYLFRGALDC RARRIDTGML
LAAVDALADL AREPVSDAVL AAYDLAPDSL RFGPEYIIPK ALDPRLRERV AAAVAAAARR
SGQARR
//