ID A0A132BU95_9RHOB Unreviewed; 759 AA.
AC A0A132BU95;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:KUP91320.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KUP91320.1};
GN Name=maeB {ECO:0000313|EMBL:KUP91320.1};
GN ORFNames=TRIHO_38940 {ECO:0000313|EMBL:KUP91320.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP91320.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP91320.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP91320.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-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:KUP91320.1}.
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DR EMBL; LPUY01000100; KUP91320.1; -; Genomic_DNA.
DR RefSeq; WP_068247679.1; NZ_LPUY01000100.1.
DR AlphaFoldDB; A0A132BU95; -.
DR PATRIC; fig|1768241.3.peg.4061; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000068382; 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:KUP91320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068382}.
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; 82321 MW; FC7EC615F573D333 CRC64;
MTDKTSESLR DAALHYHEFP RPGKLEIRAT KPLATGYDLA RAYSPGVAEA CLEIKDDEAN
AARYTARGNL VAVVSNGSAV LGLGNIGALA SKPVMEGKAV LFKNFANIDC FDIEVNETDP
EKLADIVCAL EPTFGAINLE DIKAPDCFIV EKLCRERMNI PVFHDDQHGT AIVVGAAATN
ALFVAKKRFD EIKIVSTGGG AAGIACLNML LKLGVKRENI WLCDIHGVVH QGRKEDMNPQ
KAAFAQATDK RTLDEVIDGA DLFLGLSGPN VLTPEMVKKM AQRPIVFALA NPTPEIMPDL
ARAVVPDAII ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT EINDEMQIAC VEGIAELART
TTSAEAAAAY KGEQLTFGAD YLIPKPFDPR LVAVVSTAVA TAAMKSGVAK RPIEDLSAYR
AKLNQSVFKS ALLMKPVFEA ARAASRRIVF AEGEDERVLR AAQEILRETT ETPILIGRPD
VIEARAERLG LSIRVGEDVE IVNPENDPRY REYWTSYHQI MERQGVTPDL AKAILRTNTT
AIGAIMVHRE EADSLICGTF GEYRWHLNYV TQILGGGTYA PHGALSMMIL EDGPLFIADT
QVRIELTPEE IAQTVIGAAR HVRRFGIKPQ IALCSQSQFG NIPCDTGARL RGALEILDSR
PRDFIYEGEM NIDTALDPNL RDRIFPNSRL EGAANVLIFA HADAASGVRN ILKMRSGGLE
VGPILMGMGN RAHIVSQSIT ARGLLNMAAI AGTPVGHYS
//
