ID A0A399J2V1_9RHOB Unreviewed; 760 AA.
AC A0A399J2V1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RII38789.1};
GN ORFNames=DL237_11135 {ECO:0000313|EMBL:RII38789.1};
OS Pseudooceanicola sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2211117 {ECO:0000313|EMBL:RII38789.1, ECO:0000313|Proteomes:UP000265848};
RN [1] {ECO:0000313|EMBL:RII38789.1, ECO:0000313|Proteomes:UP000265848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY03 {ECO:0000313|EMBL:RII38789.1,
RC ECO:0000313|Proteomes:UP000265848};
RA Zhang Y.-J.;
RT "Pseudooceanicola sediminis CY03 in the family Rhodobacteracea.";
RL Submitted (AUG-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}.
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:RII38789.1}.
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DR EMBL; QWJJ01000008; RII38789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399J2V1; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000265848; 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 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 760 AA; 81622 MW; 91ECC7B5BB598D7B CRC64;
MSDTDKTTLR DAALAYHEFP KPGKLEVRAT KPLANGRDLS LAYSPGVAEA CLEIKADPSA
ASRYTARGNL VAVVSNGTAV LGLGNIGALA SKPVMEGKAV LFKKFAGIDC FDIELDESDP
EKLADIVCAL GPTFGAINLE DIKAPDCFIV EKICRERMNI PVFHDDQHGT AIVVGAAATN
ALRVANKNFE DIKIVSTGGG AAGIACLNML VKLGVKRENI WLCDIHGLVH EGRNEDMNPH
KAAFAQASDL RTLDEVIDGA DLFLGLSGPG VLTAEQVGRM TKKQPIIFAL ANPTPEIMPD
LARAVAPDAI IATGRSDFPN QVNNVLCFPF IFRGALDVGA TEINDEMQIA CIEGIAALAR
ATTSAEAAAA YQGERLTFGT DYLIPKPFDP RLSGIVSSAV AKAAMESGVA TRPIDDLAAY
KAKLNSSVFK SAMLMRPVFE AAQTASRRIV FAEGEDERVL RAAQAILEET TEQPILIGRP
EVIESRCNRA GLKIKPGVDF HVVNPENDPR YRDYWMTYHK LMARRGVTPE VARAIMRTNT
TAIGAIMVHR EEADSLICGM FGEYRWHLNY VTQVLGGGAR QPTGALSMMI LEDGPLFLTD
THINPDPTPG QIAAAAIGAA RHVKRFGLLP KIALCSRSQF GNQDTESAMR MRLAMEILDS
EPRDFMYEGE MNVDTALDAR LREEVFPESR LEGAANALVF GHADTASGVR NILKTKGGGL
EVGPILMGMR NCAHIVSAST TARGLLNMAA IAGTPVAHYG
//
