ID L0JKY5_NATP1 Unreviewed; 751 AA.
AC L0JKY5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Malate dehydrogenase, phosphate acetyltransferase {ECO:0000313|EMBL:ELY73433.1};
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:AGB31503.1};
GN OrderedLocusNames=Natpe_1606 {ECO:0000313|EMBL:AGB31503.1};
GN ORFNames=C488_13581 {ECO:0000313|EMBL:ELY73433.1};
OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS 786 / 157).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB31503.1, ECO:0000313|Proteomes:UP000010843};
RN [1] {ECO:0000313|Proteomes:UP000010843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC {ECO:0000313|Proteomes:UP000010843};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGB31503.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB31503.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ELY73433.1, ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY73433.1,
RC ECO:0000313|Proteomes:UP000011593};
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).
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 ---------------------------------------------------------------------------
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; CP003372; AGB31503.1; -; Genomic_DNA.
DR EMBL; AOIE01000077; ELY73433.1; -; Genomic_DNA.
DR RefSeq; WP_006182080.1; NZ_AOIE01000077.1.
DR AlphaFoldDB; L0JKY5; -.
DR STRING; 797303.Natpe_1606; -.
DR GeneID; 14332347; -.
DR KEGG; npe:Natpe_1606; -.
DR PATRIC; fig|797303.5.peg.2743; -.
DR eggNOG; arCOG00853; Archaea.
DR HOGENOM; CLU_012366_0_0_2; -.
DR OrthoDB; 45556at2157; -.
DR Proteomes; UP000010843; Chromosome.
DR Proteomes; UP000011593; 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; 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 Transferase {ECO:0000313|EMBL:ELY73433.1}.
FT DOMAIN 14..147
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 159..399
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 751 AA; 81024 MW; C153D637F7AFCD07 CRC64;
MDEDALEYHR TDPPGKIEIS TTKPTNTQRD LSLAYSPGVA APCLEIDEDE TDAYQYTTKG
NLVGVVSNGS AVLGLGDIGA QASKPVMEGK GVLFKRFADI DVFDIELELD DTDAFVEAVA
AMEPTFGGIN LEDIAAPECF EIEERLRERL SIPVFHDDQH GTAIITGAAL LNAVEISGKD
LADLEVTVAG AGAAAVATAR FYVSLGVRRE NITMVDIDGI LTTERAEAGD LNEYNRQFAS
DVPEGELADA MVGADAFVGL STGGIVSQEM VRSMAEDPII FAMANPEPEI DYESAKAARD
DTVIMATGRS DYPNQVNNVL GFPFLFRGAL DVRATEINEA MKVAAAHALA ELAKQDVPDA
VVKAYGDQPL QFGPDYIIPK PLDTRVLFEV APAVARAAID SGAARVEFDV DAYVERLEAR
LGKSREMMRV VLNKAKSDPK RIALAEGTDE TIVRAAAQMA DRGVAEPVLI GDAAEIERTV
ADLALEFDPD VVDPGSGDYG EYVDHLYERR RRNGVTRREA ETMIRDDTNY FGSVMVDRGD
ADAMLTGLTN HYPSALRPPL QVIGTADDAD YAAGVYMLTF KNRVVFVADA TVNQAPDADV
LEEVTRHTAD LARRFDVDPR AALLSYSDFG SVDNEGTRKP REAAQRLRDD PAVAFPVDGE
MQADTAVVEE MLTGTYEFTD LEKPANVLVF PNLEAGNIGY KLLQRLGGAE AIGPMLVGMD
EPVHVLQRGD EVKDIVNLAA VATVDAQGDE S
//
