ID A0A0J9EG93_9RHOB Unreviewed; 759 AA.
AC A0A0J9EG93;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:KMW60684.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KMW60684.1};
GN ORFNames=AIOL_000848 {ECO:0000313|EMBL:KMW60684.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW60684.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW60684.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW60684.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) 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:KMW60684.1}.
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DR EMBL; LFTY01000001; KMW60684.1; -; Genomic_DNA.
DR RefSeq; WP_049641731.1; NZ_LFTY01000001.1.
DR AlphaFoldDB; A0A0J9EG93; -.
DR STRING; 1675527.AIOL_000848; -.
DR PATRIC; fig|1675527.3.peg.906; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KMW60684.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178}.
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 REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 82314 MW; 3704939545538CAB CRC64;
MTENRQDSFR QQALTYHEEP RPGKLEIRPT KPMANGRDLS LAYSPGVAEA CLEIKADPAN
ASRYTARANL VAVVSNGSAV LGLGDIGVAA SKPVMEGKAV LFKKFAGIDC FDIELNESDP
EKLADIVCAL EPTFGAINLE DIKAPDCFIV EKLCRERMNI PVFHDDQHGT AIVVGAAATN
ALRVADKDWA DIKVVSTGGG AAGIACLNML LKLGVRRENV YLVDLHGLVH EGREQDMTPQ
KAEYAQKGGA RPLAEVIEGA DLFLGLSGPK VLTPEMVKSM APKPIIFALA NPEPEIMPDL
ARDAVEDAII ATGRSDFPNQ VNNVLCFPFI FRGALDVGAR EINDQMKLAC IDAIAELARA
STSAEAAAAY RGERMTFGPD YLIPKAFDPR LTGVIATAVA KAAMESGVAT REIVDFGAYR
KKLDGSVFRS ALIMRPVFDA AATAERKIVF TEGEDERVLR AANAMIEETT DKPILIGRPA
VVEQRLERAG LPIRPGRDFE LVNPERDTRY HHYWTTYHRI MQRKGVTPDL ARAILRTNTT
AIGAVMVHRG DADSMICGTF GQFLWHLNYI QQVLGNAELH PVGALSLMIM GDGPLFIADT
QVHPEPTPAQ IAETVIACAR HIRRFGVEPK IAMCSHSQFG NLDCGTGERM RGALEILDAE
KRDFAYEGEM HADSALDEEL RDRIFPNARF RGPANCLVFA NTDATSGVRN ILKMKAGGLE
VGPILMGMGN RAHIATPSIT ARGLLNMSAI AGTPVAHYG
//
