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Database: UniProt
Entry: A0A3T0N136_9RHOB
LinkDB: A0A3T0N136_9RHOB
Original site: A0A3T0N136_9RHOB 
ID   A0A3T0N136_9RHOB        Unreviewed;       757 AA.
AC   A0A3T0N136;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AZV77725.1};
GN   ORFNames=EBB79_07360 {ECO:0000313|EMBL:AZV77725.1};
OS   Parasedimentitalea marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Parasedimentitalea.
OX   NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV77725.1, ECO:0000313|Proteomes:UP000283063};
RN   [1] {ECO:0000313|EMBL:AZV77725.1, ECO:0000313|Proteomes:UP000283063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W43 {ECO:0000313|EMBL:AZV77725.1,
RC   ECO:0000313|Proteomes:UP000283063};
RA   Cao J.;
RT   "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT   from deep seawater of the New Britain Trench.";
RL   Submitted (OCT-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}.
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DR   EMBL; CP033219; AZV77725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3T0N136; -.
DR   KEGG; sedi:EBB79_07360; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000283063; 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:UniProtKB-KW.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          20..153
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          165..402
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         78..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         164
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         289
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   757 AA;  82101 MW;  900823ECE7D58E7B CRC64;
     MPDTQNLRQA ALHYHEYPQP GKLEIRATKP MANGRDLARA YSPGVAEACT EIKTDPANAA
     RYTSRGNLVA VVTNGTAVLG LGNIGALASK PVMEGKAVLF KNFAGIDCFD IELDESDPEK
     LADIVCALEP TFGAINLEDI KAPDCFIVEK ICRERMNIPV FHDDQHGTAI VVGAAARNAL
     HVAGKSFEDI KIVSTGGGAA GIACLNMLLK LGVKRENIWL CDIHGLVYEG RVEDMNPHKA
     AFAQATDKRT LDDVIGEADL FLGLSGPNVL KPEMVAKMSD RPIIFALANP NPEIMPDTAR
     KVKPDAIIAT GRSDFPNQVN NVLCFPFIFR GALDVGATEI NDAMQIACVE GIAELARATT
     SAEAAAAYKG EQLTFGADYL IPKPFDPRLV AVVSSAVAKA AMETGVAARQ IEDMAIYKQK
     LNQTVFKSAL LMKPVFEAAR VASRRIVFAE GEDERVLRAA QAILEETTET PILIGRPEVI
     DARCEKLGLD IRPGSDFQIV NPENDPRYYD YWNSYHRLLQ RQGVTPDIAK AVMRTNTTAI
     GAIMVHRGEA DSLICGTFGE YRWHLNYVSQ MLGGDSYEPH GALSLMILED GPLFIADTHV
     RVEPTPEQIA QSVIGAARHV RRFGLEPKIA LCSQSQFGNT NCDTGARLRA ALEILDDKQR
     DFVYEGEMNI DTALDADLRT RIFPNSRMEG AANVLIFAHA DAASGVRNIL KMRADGLEVG
     PILMGMGNRA HIVSPSITAR GLLNMAAIAG TPVTHYG
//
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