ID V4GRV5_9EURY Unreviewed; 752 AA.
AC V4GRV5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Bifunctional malic enzyme oxidoreductase/phosphotransacetylase {ECO:0000313|EMBL:ESP87786.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ESP87786.1};
GN ORFNames=K933_12356 {ECO:0000313|EMBL:ESP87786.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP87786.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP87786.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP87786.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain G22,
RT Isolated from the Hypersaline Waters of Lake Tyrrell, Australia.";
RL Genome Announc. 1:e01001-13(2013).
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:ESP87786.1}.
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DR EMBL; ASGZ01000044; ESP87786.1; -; Genomic_DNA.
DR RefSeq; WP_023395047.1; NZ_ASGZ01000044.1.
DR AlphaFoldDB; V4GRV5; -.
DR STRING; 1324957.K933_12356; -.
DR PATRIC; fig|1324957.4.peg.2510; -.
DR eggNOG; arCOG00853; Archaea.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000017840; 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:ESP87786.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017840}.
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..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 81162 MW; C51A25FEA517FAEB CRC64;
MGLDDDAREY HRSDPPGKIE ISTTKPTNTQ RDLSLAYSPG VAAPCLDIDA DSERAYEYTA
KGNLVAVVSN GSAVLGLGDI GGQASKPVME GKGVLFKRFA DIDVFDIELD QTDPDDIIRS
VSAMEPTFGG VNLEDIAAPE CFEIESKLRE EMDVPVFHDD QHGTAIISGA ALINAADIVD
KDLSELDIVF SGAGASAIAT ARFYVSLGAE ASNIVMCDSS GVITAERAAN DDVNEFKKEF
ASETAEGGLA DAMEGADVFV GLSVGGIVDQ EMVRSMADDP VIFAMANPDP EIGYEEAKNA
RDDTVIMATG RSDYPNQVNN VLGFPFIFRG ALDVRATDIN EEMKRAAAEA LADLARQDVP
DAVVKAYGDQ PLQYGPEYVI PKPLDPRVLF ELAPAVAEAA SESGVARTEL DPDEYTERLE
ARLGKGREMM RVVLNKARSE PKRVVLAEGA DEKMIRAAYQ MREQGIADPV LLGDRGEIES
TARRLGLGFD PEVVDPGEDA AADRYADRLH DLRKRKGITR SEAADLVQRD SNYFGSVMVE
EGDADALLTG LTHDYPKALR PPLQVIGTAE DADYVAGVYM LTFKNRVVFC ADTTVNQAPD
EEVLAEITKH TADLARRFNV EPRAAMLSYS NFGSVENEGT MKPRKAVERL HDDPEVDFPV
DGEMQADTAV VEEILEDTYP FAELDGPANV LVFPNLEAGN IGYKLLQRLG GAGAIGPMLV
GMDKPVHVIQ RGDEVKDIVN LAGVAVVDAQ DE
//
