ID A0A1Z9WH63_9GAMM Unreviewed; 757 AA.
AC A0A1Z9WH63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:OUX76977.1};
GN ORFNames=CBC19_08155 {ECO:0000313|EMBL:OUX76977.1};
OS Oceanospirillales bacterium TMED59.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1986765 {ECO:0000313|EMBL:OUX76977.1, ECO:0000313|Proteomes:UP000195499};
RN [1] {ECO:0000313|EMBL:OUX76977.1, ECO:0000313|Proteomes:UP000195499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED59 {ECO:0000313|EMBL:OUX76977.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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}.
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:OUX76977.1}.
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DR EMBL; NHDM01000065; OUX76977.1; -; Genomic_DNA.
DR Proteomes; UP000195499; 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: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 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 757 AA; 81723 MW; BE5C8D6F74FCC15A CRC64;
MSNDLREAAL RYHRAEPAGK LEIAATKPMA TQRDLALAYS PGVAYACTEI AEDPSKAAEL
TARGNMVAVI TNGTAVLGLG AIGPLASKPV MEGKSVLFKK FANINSIDIE VDTTDVDRFC
DVVSALEPSF GGINLEDIKA PECFEIETRL REKMNIPVFH DDQHGTAIVV GAGMLNAMRY
LGKEMGEIKL VCSGAGAAAL ACLNMLKTLG VKQENITVCD QHGVLRTGRE KPMDKYKTQY
ARETDLKTLK EALVGADAFL GLSVPGVIDQ DDIKNMADRP VIFALANPTP EIMPEVVKEV
RPDALIATGR SDYPNQVNNV LCFPFLFRAA LDCGATVINE EMKAACAEAI AAMVHSPPSD
EVLNTYQGEQ LTFGPEYLIP KPFDPRLIME IPPGVAXAAA KSGVAMRPIQ DLDAYRDDLS
RFVFRSGMLM KPMFEAARAT KRRLVLAEGE GGKMLQACQL IVSENLADVT LVGRRKVIEE
KIQSMXLSIQ AGKDFQIVDN LDDAVITPIG EEYHALMARQ GMTPKAAQTR VRANTTVVAS
MLLRRGDADA MLCGTFGTYG KHLRLAEEXI GRRDGSPVVG AMTVLIXPQG TIFLTDTXVN
FDPTAEXLCE LGKLAADEIR RFGIQPKAAF LSHSNFGSSD TTSAKKVREA TTMFMDRYXX
IEADGEMHAD AALDEKVRLD LLPNSKLTGK ANLLICPNLD SANIARNLLK VLGNGVTVGP
LLLGLEKEAH VATASNSPRG IXNMAAVALA NVNRNDD
//
