ID A0A1G9Z395_9EURY Unreviewed; 754 AA.
AC A0A1G9Z395;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SDN15251.1};
GN ORFNames=SAMN05192554_11758 {ECO:0000313|EMBL:SDN15251.1};
OS Haloarchaeobius iranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halorubellaceae; Haloarchaeobius.
OX NCBI_TaxID=996166 {ECO:0000313|EMBL:SDN15251.1, ECO:0000313|Proteomes:UP000199370};
RN [1] {ECO:0000313|EMBL:SDN15251.1, ECO:0000313|Proteomes:UP000199370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC {ECO:0000313|Proteomes:UP000199370};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; FNIA01000017; SDN15251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9Z395; -.
DR STRING; 996166.SAMN05192554_11758; -.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000199370; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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: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:UP000199370}.
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..31
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 754 AA; 81879 MW; B39DD698C23379F6 CRC64;
MGLDEDSLDY HEADPPGKLE ISTTKPTNTQ RDLSLAYSPG VAEPCRRIAD DPDDAYRYTA
KGNLVGVVSN GSAVLGLGDI GAQASKPVME GKGVLFKRFA DIDVFDVELD QDDPEKIIEA
VSAMEPTFGG INLEDISAPE CFTIEETLRE EMDIPVFHDD QHGTAIISGA ALLNAAEIAG
KDLEDLEIVF SGAGASALAT ARFYVSLGAK RENITMCDSS GIITTARAES GDVNEYKQEF
ARDIDGGGLA DAMADSDVFV GLSIGGLVDQ EMVRSMADNP IVFAMANPDP EIGYEEAKAA
RDDTVIMATG RSDYPNQVNN VLGFPFIFRG ALDVRATEIN EEMKVAAASA LAELSKQDVP
DAVVKAYGDQ PLQFGPDYII PKPLDPRVLF EVAPAVAEAA MDSGCARQEL DLEAYEERLE
ARLGKSREMM RVVLNKAKSD PKRIALAEGA DEKMIRAAYQ LEEQGIAEPI LIGNDDRITK
TTERLGLDFE PTIANPRADD ERHEDYAERL YQVRKRKGLT KSEAEDLIRR DTNYYGSVMV
ECGDADALLT GLTHHYPSAL RPPLQVIGTA EEADFAAGVY MLTFKNRVIF CADTTVNQDP
DAKVLAEVAD HTAELARRFN VDPRVAMLSY SNFGSVDNAG TRKPRRAADM LRNDDGIDYP
VDGEMQADTA VVEEILRGTY EFSDLEDPAN VLVFPNLEAG NIGYKLLQRL GGAEAIGPML
VGMDKPVHVL QRGDEVKDIV NLAGVAVVDA QQNE
//