ID L0ACK2_NATGS Unreviewed; 751 AA.
AC L0ACK2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:AFZ71613.1, ECO:0000313|EMBL:ELY66668.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ELY66668.1};
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:PLK21380.1};
GN OrderedLocusNames=Natgr_0356 {ECO:0000313|EMBL:AFZ71613.1};
GN ORFNames=C490_12887 {ECO:0000313|EMBL:ELY66668.1}, CYV19_04905
GN {ECO:0000313|EMBL:PLK21380.1};
OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS 104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronobacterium.
OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ71613.1, ECO:0000313|Proteomes:UP000010468};
RN [1] {ECO:0000313|Proteomes:UP000010468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC {ECO:0000313|Proteomes:UP000010468};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFZ71613.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ71613.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Natronobacterium gregoryi SP2.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY66668.1, ECO:0000313|Proteomes:UP000011613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:ELY66668.1,
RC ECO:0000313|Proteomes:UP000011613};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:PLK21380.1, ECO:0000313|Proteomes:UP000234484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:PLK21380.1,
RC ECO:0000313|Proteomes:UP000234484};
RC TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK21380.1};
RA Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA Huang J.;
RT "The characterization of oligonucleotides binding to NgAgo.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; CP003377; AFZ71613.1; -; Genomic_DNA.
DR EMBL; AOIC01000089; ELY66668.1; -; Genomic_DNA.
DR EMBL; PKKI01000009; PLK21380.1; -; Genomic_DNA.
DR RefSeq; WP_005580203.1; NZ_PKKI01000009.1.
DR AlphaFoldDB; L0ACK2; -.
DR STRING; 797304.Natgr_0356; -.
DR GeneID; 14207520; -.
DR KEGG; nge:Natgr_0356; -.
DR PATRIC; fig|797304.7.peg.2625; -.
DR eggNOG; arCOG00853; Archaea.
DR HOGENOM; CLU_012366_0_0_2; -.
DR Proteomes; UP000010468; Chromosome.
DR Proteomes; UP000011613; Unassembled WGS sequence.
DR Proteomes; UP000234484; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
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 Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000313|EMBL:ELY66668.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010468}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 81569 MW; DB8303232ADAA701 CRC64;
MGLDEDSLDY HRTDPPGKIE ISTTKSTNTQ RDLSLAYSPG VAAPCMEIDE EEDEAYTYTA
KGNLVGVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDVELD EADPHKFVEA
VKMMEPTFGG INLEDIKAPE CFTIEERLRE ETDIPVFHDD QHGTAIISGA ALLNAADVAD
KDLEDLEIVF SGAGASAIAT AKFYVSLGCR KENVTMCDSS GIITEERAEN GELNEYKRQF
ARDVPEGDLA DAMEGADVFV GLSIGGIVSQ QMIQSMADDP IVFAMANPDP EIGYEEAKEA
RDDTVIMATG RSDYPNQVNN VLGFPFIFRG ALDVRATEIN EAMKVACAEA LAELAREDVP
DAVVKAYGDE PLQFGSDYII PKPVDPRVLF RVAPAVAEAA IESGAARTEI DPDEYEEELE
ARLGKSREMM RVVLNKAKTD PKTVALAEGE NEKIIRAAYQ IQEQGIAAPI LIGDESEIRQ
TAANLGLDFE PQVADPAVGD YEEYADRLHE LRARKGITRT EAGDLIERDS NYFGTVMVEQ
GDADALLTGL SYHYPSALRP PLQVIGTADD VDYAAGVYML TFKNRVVFVA DATVNQDPDE
EVLAEVTRLT GELARRFNVE PRAALLSYSN FGSVDNQGTR KPRRAAHMLQ DDPEVDFPVD
GEMQADTAVV EDILQGTYGF SELEEPANVL VFPNLESGNI GYKLLQRLGG ADAIGPMLVG
MDKPVHVLQR GDEVKDIVNL ASVAVVDAQQ E
//
