ID A0A0M2R668_9PROT Unreviewed; 763 AA.
AC A0A0M2R668;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KKJ77151.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KKJ77151.1};
GN ORFNames=WH95_08770 {ECO:0000313|EMBL:KKJ77151.1};
OS Kiloniella litopenaei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Kiloniella.
OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ77151.1, ECO:0000313|Proteomes:UP000034491};
RN [1] {ECO:0000313|EMBL:KKJ77151.1, ECO:0000313|Proteomes:UP000034491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ77151.1,
RC ECO:0000313|Proteomes:UP000034491};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut microflora
RT of Pacific white shrimp, Penaeus vannamei.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KKJ77151.1}.
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DR EMBL; LANI01000005; KKJ77151.1; -; Genomic_DNA.
DR RefSeq; WP_046505740.1; NZ_LANI01000005.1.
DR AlphaFoldDB; A0A0M2R668; -.
DR STRING; 1549748.WH95_08770; -.
DR PATRIC; fig|1549748.8.peg.3770; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000034491; 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; IPR015884; Malic_enzyme_CS.
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.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW 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:KKJ77151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034491}.
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 763 AA; 82687 MW; 9B194EBABE9C8E5B CRC64;
MPKHNSRTTD ADALDFHASG RPGKLEIKAT KPLTTQRDLS LAYSPGVAVP CLEIAKNPAA
AYDYTAKGNL VAVISNGTAV LGLGNLGALG SKPVMEGKAV LFKRFADVDG IDLEVDTENV
DEFVNCVRFL GKSFGGINLE DIKAPECFII EQRLQELLDI PVFHDDQHGT AIIAAAGLLS
AIDITGKDLK KIKMVVNGAG SAGIACTELV KALGVPHENI LLCDTKGVIY QGREEGMNQW
KSAHAVPTDD RTLEDAMNSA DVVFGLSVKG AFTNDMIKSM APNPIIFAMA NPDPEITPEE
VAKVRDDAII ATGRSDYPNQ VNNVLGFPYI FRGALDVRAS SINMEMKVAA AKALAELAQE
DVPDEVGKAY AGRQLKYGRD YIIPAPFDPR LVAVIPRAVA EAAMESGVAG KNIEDLDAYE
RELSARLDPA ATTFMRIAQK VRSNPKRVVF AEGEEESAIR AAVTYYNAGY GTPLLVGREE
TIKNTMQRLG INGDFIEIHN ASISEHRERY TDYVYNRLQR KGKLYRDCQR MVNQNRNIFA
SCLVTDGIAD AMVTGLTRSF AVSLDDAMRA INCKPGKRAM GMSMMIIDGK AIFVADTSVN
EVPSSEQLAD IAVQAASHVQ AMGYEPRVAF LSFSNFGNPT RETTTRIRRA VSVLDTMNVS
FEYEGEMQAN LALDFELQQR LFPFSRLTGP ANILIMPALH SANITTKLIQ KAGGSTAVIG
PMLVGLEKPV QIVPMGATVT DLVTMAALGA YESITNEMEE PFL
//
