ID A0A0R2T7S6_9FLAO Unreviewed; 762 AA.
AC A0A0R2T7S6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KRO82824.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KRO82824.1};
GN ORFNames=ABR87_06895 {ECO:0000313|EMBL:KRO82824.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO82824.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO82824.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO82824.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO82824.1}.
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DR EMBL; LICF01000018; KRO82824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2T7S6; -.
DR Proteomes; UP000051535; 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:0000313|EMBL:KRO82824.1}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..403
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
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 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 762 AA; 83422 MW; 549395353E7EC133 CRC64;
MAKKNAPIRK RDILDYHEGP RPGKIEVIPT KPSNSQRDLS IAYSPGVAEP CLEIAANPSD
AYRYTAKGNL VAVISNGTAV LGLGDIGALA SKPVMEGKGV LFKIFADIDV FDLELDTKDP
EKFIETVKIL APTFGGINLE DISAPECFEI ERRLREELDI PVMHDDQHGT AIITGAALLN
ALEIVQKDIK QVKVVFNGAG ASAISCATLY LVLGVDPKNL IMCDSKGVIH SGRTGLTHEK
LGFARDTPLR ELSEAMDGAD VFVGLSKGNI LTPDMIKTMA KDPIVFALAN PDPEIQYDIA
KSTRDDLIMA TGRSDNPNQV NNVLGFPYIF RGALDVRATR INEAMKLAAV RAIADLAKEP
VPEIVNLAYG SRNMTFGQDY IIPKPFDPRL IYKVSSAVAR AAMESGVAQT SIANWDAYEE
ELRSRLGRDD KFIRLVMEKA KTHPKKVVFN EADNYRVLKA AQIVLEEGIA EPILLGDASR
IQALNEAYAL GLEEVQVIDV KSLHVPQIEA YADAYYKVRQ RKGVGFDEAR RNMRNRDYYG
PMMVLMGDAD AYITGSMVKY PRAVKPVLEI LGPKDPSRTV AGVYVMLTKR GPRFFADTTM
NQDPSAERVA QIACEAAAMV RKMNIEPRVA LLSYSNFGSS VDGKTPRKMR EALRIIRERE
PGLIADGEMQ ANFAVDNTLL QEQFPFSDLV GKEPNIFVFP GLSSANISYK LLQSMGSMEA
VGPLLIGLSY PAHVLQLGSS VREIVNAAAM AVIDAQSREA ID
//
