ID A0A159Z7S0_9RHOB Unreviewed; 774 AA.
AC A0A159Z7S0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:AMY70668.1};
GN ORFNames=AKL17_3443 {ECO:0000313|EMBL:AMY70668.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY70668.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY70668.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-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}.
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DR EMBL; CP012661; AMY70668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A159Z7S0; -.
DR STRING; 1335048.AKL17_3443; -.
DR KEGG; daa:AKL17_3443; -.
DR PATRIC; fig|1335048.3.peg.3567; -.
DR Proteomes; UP000076128; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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}.
FT DOMAIN 37..170
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 182..419
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 95..102
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 774 AA; 83351 MW; F06626F9D9353DC3 CRC64;
MDDMNEDATP QAGARLDEAR HDKARLDALR YHEEPKPGKL EIRATKPLAN GRDLSLAYSP
GVAEACLEIK ADPATAARYT SRGNLVAVVS NGTAVLGLGN IGPLAAKPVM EGKAVLFKKF
ANIDCFDIEL NEMDPVKLAD IVCAMEPSFG AINLEDIKAP DCFIVEKLCR ERMNIPVFHD
DQHGTAIVVG AAATNALHVS GKRFEDIKVV STGGGAAGIA CLNMLLKLGV RRENVWLCDL
AGLVYRGREA EMTPQKAEYA QGDMPRTLAE VIVGADLFLG LSGPGVVTPA MVASMAPRPI
VFALANPTPE ILPDLVRSVA PDAIIATGRS DYPNQVNNVL CFPFIFRGAL DVGATQINDA
MQIACIEGIA ALARATTSAE AAAAYSGEKM TFGADYLIPK PFDPRLMGVV AKAVARAAME
TGVATRPIED LAAYKHRLDS SVFRSAMLMR PVFEAAATVT RRIVFAEGED ERVLRAANAM
LEETTDKPIL IGRPEVIAMR AERAGLPIRP ERDFEIVNPE SDSRYRDYWE TYHGLMARRG
VSPDIARAVM RTNTTAIGAV MVHRGEADSL ICGTFGQYLW HLNYVQQVLA RDGLHPIGAL
SLMILEDGPL FIADTHVHPE PTPEQIMDCA KGAARHVKRF GLAPKIALCS HSQFGNLDNS
SGRRMREALD LLDAQEVDFA YEGEMHVDAA LDQGLRDRIF PGGRFDGQAN VLIFGNSDAA
SGVRNILKMK AGGLEVGPIL MGMGNRAHVV TPSITTRGLL NMSALAGTPV AHYG
//
