ID A0A433RZI8_9RHOB Unreviewed; 759 AA.
AC A0A433RZI8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:RUS58711.1};
GN ORFNames=EGN72_17415 {ECO:0000313|EMBL:RUS58711.1};
OS Pseudorhodobacter sp. E13.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2487931 {ECO:0000313|EMBL:RUS58711.1, ECO:0000313|Proteomes:UP000267424};
RN [1] {ECO:0000313|EMBL:RUS58711.1, ECO:0000313|Proteomes:UP000267424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E13 {ECO:0000313|EMBL:RUS58711.1,
RC ECO:0000313|Proteomes:UP000267424};
RA Lee H., Kim S.;
RT "Pseudorhodobacter sp. isolated from seawater.";
RL Submitted (NOV-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:RUS58711.1}.
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DR EMBL; RPEN01000159; RUS58711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433RZI8; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000267424; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000267424}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..404
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 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 759 AA; 81941 MW; F39B86A89A7C214D CRC64;
MDETRQDTQR QAALNYHEFP KPGKLEIRAT KPLANGRDLA LAYSPGVAEA CLEIKADPST
ATRYTSKGNL VAVVSNGTAV LGLGNIGALA SKPVMEGKAV LFKKFANIDC FDIELNEPDP
YKLADIVCAL EPTFGAINLE DIKAPDCFIV ESICRERMGI PVFHDDQHGT AIVVGAAATN
ALHVAGKKFE DIKIVSTGGG AAGIACLNML LKLGVKRENV WLCDIKGLVY EGRTEDMTPQ
KAEYAQKSDK RTLADVIEGA DLFLGLSGPG VLKPDMVARM AKRPIVFALA NPTPEITPDE
ARAVVPDVIM ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT TINDEMKIAC IEGIAALARA
TTSAEAAAAY KGEQLTFGPD YLIPKPFDPR LIGVVASAVA KAAIETGVAT KQIEDFDAYK
RKLDSSVFRS ALIMRPVFQA AATATRRIVF AEGEDERVLR AANAMIEETT DKPILIGRPE
VVESRCERAG LPIRPGRDFD LVNPENDPRY RDYWETYHQL MARKGVTPDI ARAVMRTNTT
AIAAVMVHRD EADSMICGTF GQYLWHLNYV TQVLATEGRH PVGALSLMIL EDGPLFIADT
HVHPDPTPEQ ITETVIGAAR HVRRFGLVPK VALLSSSQFG NLNCETGRRM RAAIDVLDAA
PRDFCYEGEM HIDAALDQAT RDRIFPGGRF EGPANVLIFA NSDAASGVRN ILKMRGGGLE
VGPILMGMGN KAHIVTPSIT ARGLLNMSAL AGTPVATYG
//
