ID A0A1H5V283_9EURY Unreviewed; 747 AA.
AC A0A1H5V283;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:QCC46865.1, ECO:0000313|EMBL:SEF80527.1};
GN ORFNames=DV707_03820 {ECO:0000313|EMBL:QCC46865.1}, SAMN04488133_0793
GN {ECO:0000313|EMBL:SEF80527.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEF80527.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEF80527.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEF80527.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC46865.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC46865.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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; CP031311; QCC46865.1; -; Genomic_DNA.
DR EMBL; FNVN01000001; SEF80527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5V283; -.
DR KEGG; hlm:DV707_03820; -.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000236740}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..398
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..27
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 747 AA; 80716 MW; 8DBA3A6641739EFC CRC64;
MGLDDDAREY HREEPPGKIE ISTTKPTNTQ RDLSLAYSPG VAAPCRDIDA DPTRAYEYTA
KGNLVGVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDVELD LDDPDDIVDT
VRAMEPTFGG INLEDIKAPE CFEIESRLRE EVDIPVFHDD QHGTAIISGA ALLNAADVVD
KDLGELNVVF SGAGASAIAT ARFYTSLGVE TENITMCDSS GVIGTDREDL NEFKAQFASD
TDDDTLAEAL AGADVFVGLS VGGIVSQEMV ASMAENPIVF AMANPDPEIE YETAKAARDD
TVIMATGRSD YPNQVNNVLG FPFIFRGALD VRATEINEDM KRAAAEALAD LARQDVPDAV
VKAYGDQPLQ FGPDYVIPKP LDPRVLFEVA PAVAEAAMDS GCARTEVDLD AYEERLEARL
GKSREMMRVV LNKAKSDPKR VALAEGGDEK MIRAAYQMRE QGIAHPVLVG DTDEITSTAA
DLGLDFEPEV ADPWAGEWDH YADRLYELQQ RKGVTKREAH ELIRGDSNYL ASVMVEEGDA
DAMLTGLTHH YPSALRPPLS IIGTAPDADY AAGVYMLTFK NRVVFAADTT VNLDPDSDVL
AEITKHTAEL ARRFNVEPRA AMLSYSNFGS VDNEGTRKIR DAVSELHADA EVDFPVDGEM
QADTAVVEDI LEGTYEFSQL DQPANVLVFP NLEAGNIGYK LLQRLGGAEA IGPMLVGMDK
PVHVLQRGDE VKDIVNLAGV AVVDAQE
//
