ID A0A365TAJ3_9EURY Unreviewed; 752 AA.
AC A0A365TAJ3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RBI61743.1};
GN ORFNames=DMJ13_13695 {ECO:0000313|EMBL:RBI61743.1};
OS halophilic archaeon.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=29295 {ECO:0000313|EMBL:RBI61743.1, ECO:0000313|Proteomes:UP000252983};
RN [1] {ECO:0000313|EMBL:RBI61743.1, ECO:0000313|Proteomes:UP000252983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H22 {ECO:0000313|EMBL:RBI61743.1,
RC ECO:0000313|Proteomes:UP000252983};
RA Chen S.;
RT "Draft genome sequence of Haloarchaeon sp. H22 isolated from a salt mine.";
RL Submitted (JUL-2018) 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}.
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:RBI61743.1}.
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; QNGA01000003; RBI61743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365TAJ3; -.
DR Proteomes; UP000252983; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; 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 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000252983}.
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 81136 MW; E97A8D17DC964516 CRC64;
MGLDEDSLDY HRREPPGKIE ISTTKPTNTQ RDLSLAYSPG VAAPCNEIDA DAEAAYSYTA
KGNLVGVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDLELE QADPEDIVRT
VSAMEPTFGG INLEDIKAPE CFEIEERLRE EIDIPVFHDD QHGTAIISGA ALLNATEING
KDLENLEIVF SGAGASAIAT ARFYVSLGAR KENITMCDSS GIITENRAAR GDVNEYKTEF
ARDVPEGDLA DAMAGADVFV GLSVGGIVSE EMVRSMAADP VIFAMANPDP EIGYEEAKAA
RDDTVIMATG RSDYPNMVNN VLGFPFIFRG ALDVRASDIN EDMKVAAAEA LADLAKKDVP
DAVVKAYGDQ PLQFGPDYII PKPLDPRVLF EIAPAVAEAA MESGVARSEL DTDEYVETLE
ARLGKSREMM RVVLNKAKSD PKRVALAEGT DEKMIRAAYQ IRDQGIAEPV LIGDQAEIAA
TADDLGLDFD PTVADPSTGD YEAYADRLYE LRRRKGITRS EAGELVRKDS NYFGSVMVEQ
GDADAMLTGL THHYPSALRP PLQVIGTAPD ADYAAGVYLL TFKNRVVFCA DATVNQDPDE
EVLAEITRHT AELARRFNVE PRAAMLSYSN FGSVDNEGTR KPRRAAETLR EDPSVDFPVD
GEMQADTAVV SDILNGTYEF SDLDDPANVL VFPNLEAGNI GYKLLQRLGG AEAIGPMLVG
MDKPVHVLQR GDEVKDIVNL AGVAVVDAQQ NE
//