ID W8STN4_9RHOB Unreviewed; 759 AA.
AC W8STN4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AHM05885.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:AHM05885.1};
GN ORFNames=roselon_03641 {ECO:0000313|EMBL:AHM05885.1};
OS Roseibacterium elongatum DSM 19469.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseibacterium.
OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM05885.1, ECO:0000313|Proteomes:UP000019593};
RN [1] {ECO:0000313|EMBL:AHM05885.1, ECO:0000313|Proteomes:UP000019593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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}.
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DR EMBL; CP004372; AHM05885.1; -; Genomic_DNA.
DR RefSeq; WP_025313484.1; NZ_CP004372.1.
DR AlphaFoldDB; W8STN4; -.
DR STRING; 1294273.roselon_03641; -.
DR KEGG; red:roselon_03641; -.
DR PATRIC; fig|1294273.3.peg.3595; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000019593; Chromosome.
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:AHM05885.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019593}.
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; 81410 MW; B8B572F0AB8B83D7 CRC64;
MSDEKHESLR SAALFYHEHP SPGKLEVRAT KPLANGRDLS RAYSPGVAEA SLEIKADPAN
AARYTSRGNL VAVVSNGSAV LGLGNIGALG SKPVMEGKAV LFKKFANIDC FDLEIDESDP
EKLADIVCAL EPTFGAINLE DIKAPDCFTV ERLCRERMNI PVFHDDQHGT AIVVGAAATN
ALRVVGKRFE DIKLVSTGGG AAGIACLNML LKLGLKRENV WLCDIDGLVY QGREVGMTPQ
KAEYAQGTAP KTLDEVIDGA DMFLGLSGPG VLTPEMVAKM ADRPVIFALA NPTPEILPDA
VRSVAPEAVI ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT EINDEMQIAC IKGIAALARA
TTSAEAAAAY VGEQMNFGPD YLIPKPFDPR LIAVVAGAVA EAAMASGVAT RPLDDLAAYR
DRLNQSVFRS ALIMRPVFEA ASGTTRRIVF AEGEDERVLR AAQAMLEETT DKPILIGRPE
AIDLRIERAG LTVKPGGDFE LVNPENDPRY RDYWGTYHEV MQRRGVTPDL ARAIMRTNTT
AIGAVMVHRD EADSMICGTF GQYLWHLNYV RQLLETPELT PVGALSLMIL EDGPLFVGDT
QVHPVPSPEQ IAETVIATAR HINRFGIVPQ IALCSGSQFG NLDSDSGRRM RAALDILDSE
PRAFVYEGEM HVDSALDPEL RGRVFPHSRL QGAANALIFA STDAAGATRN TLKAKAGGLE
VGPILMGMGN RAHIVTPSIT ARGLLNISAL AGTPVAHYG
//
