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Database: UniProt
Entry: F9ZLY1_ACICS
LinkDB: F9ZLY1_ACICS
Original site: F9ZLY1_ACICS 
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};
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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
//
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