ID A0A0P7WXX7_9RHOB Unreviewed; 759 AA.
AC A0A0P7WXX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:KPP92518.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KPP92518.1};
GN Name=maeB-2 {ECO:0000313|EMBL:KPP92518.1};
GN ORFNames=HLUCCA08_16505 {ECO:0000313|EMBL:KPP92518.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP92518.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KPP92518.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP92518.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(2016).
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:KPP92518.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJSF01000005; KPP92518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WXX7; -.
DR STRING; 1666913.HLUCCA08_16505; -.
DR PATRIC; fig|1666913.4.peg.1270; -.
DR Proteomes; UP000050293; 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:KPP92518.1}.
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; 81654 MW; 2F6EC49A160009FC CRC64;
MPDTPSDSLR QAALDYHRHP KPGKLEIRAT KPLANGRDLA RAYSPGVAEA SILIRDDPAT
ARDVTARGNL VAVVSNGSAV LGLGNIGALA SKPVMEGKAV LFKTFAGIDC FDIEIDETDP
EKLAEIVCAL EPTFGAINLE DIKAPDCFIV ERICRARMNI PVFHDDQHGT AIVVGAATRN
ALHVAGKRIE DIKLVSTGGG AAGIACLNML LKLGLKRENI WLCDIHGLVH QGREIDMNPQ
KAAFAQASDA RSLDEVIDGA DLFLGLSGPG VLRPDQVARM ARQPIIFALA NPTPEILPDA
ARAVAPDAII ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT EINDAMQIAC IDGIAELARA
TTSAEAAAAY KGEQLTFGAD YLIPKPFDPR LSAIVSTAVA RAAMETGVAT RPIADFDAYR
HRLNAGVFKS ALLMRPVFEA ARTAARRIVF AEGEDERVLR AAQAILEETT EKPILIGRPA
VIESRCEAAG LTIRPDRDFA VVNPENDPRY RDYWESYHRL MCRRGVTPDL ARAILRTNTT
AIGAVMVHRG EADSLICGTF GEYRWHLNYV TQVLGDDRLQ PHGALSMMIL EDGPLFLADT
QVWDLPTPEQ LAKTALGAAR HARRFGVEPR IAFCSRSQFG NQAEGSGKRL REAIALLDAM
ETDFQYEGEM NVDAALDPEL RDRLLPGGRL QGPANVLVFG HADAASGVRN ILKMKGGGLE
VGPILMGLGN RAHIVTPSIT ARGLLNMAAI AGTPVGHYG
//
