ID A0A1J0PDN9_9SYNE Unreviewed; 559 AA.
AC A0A1J0PDN9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:APD49278.1};
GN ORFNames=BM449_03565 {ECO:0000313|EMBL:APD49278.1};
OS Synechococcus sp. SynAce01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1916956 {ECO:0000313|EMBL:APD49278.1, ECO:0000313|Proteomes:UP000182608};
RN [1] {ECO:0000313|Proteomes:UP000182608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SynAce01 {ECO:0000313|Proteomes:UP000182608};
RA Tang J., Daroch M., Liang Y., Jiang D., Shah M.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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DR EMBL; CP018091; APD49278.1; -; Genomic_DNA.
DR RefSeq; WP_071801940.1; NZ_CP018091.1.
DR AlphaFoldDB; A0A1J0PDN9; -.
DR STRING; 1916956.BM449_03565; -.
DR KEGG; syny:BM449_03565; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000182608; Chromosome.
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:0008152; P:metabolic process; IEA:UniProt.
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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Reference proteome {ECO:0000313|Proteomes:UP000182608}.
FT DOMAIN 74..255
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 265..526
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 241
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 559 AA; 59179 MW; 84E73C6141BAE3C5 CRC64;
MDTLQTQLRG HQLLADPHLN KGTAFSREER QALGLDGLLP LAVETLEQQV ARVWHAFNDL
SADLEKYRFA QVLRASNATL FHRFLADHID ALLPIVYTPT VGAAIQRFSL DFRSPSGGVY
LHHQAQDHFD TILRQSARGP VDLILVTDAQ GILGLGDQGI GGVEICQGKL AVYTLCAGLD
PSRMLPVVLD VGTDNPQLRD DPLYPGCRQP RLSGGAYDAV IAAFVAAVQA AFPGALLHWE
DFGVGNARRN LDLYRAQLPS FNDDIQGTSG VATAVVLAAS RGAGMAVEDH RIVVFGAGTA
GCGIAEGLVG LLQRAGLSEA QARQRLWMID RDGLLAEGLS SIQAMAAPLA RSAAEQDSFG
RDPQGRIGLL EVVRQVHPTV LIGTSTVAGA FDQVVVEAMA AQVERPIILP LSNPTHLAEA
RPGDLLAWTG GRALVATGSP FDPVQVGGTS RRIGQCNNCF LFPGLGFACV AVGAREVSEA
MVVAGLEALA QRIPASTDPE APLMPDLSEV AAVARAVAEA VAIAAVQAGL ARLATTPEQA
IERLDQATWE PSYRPVEAI
//
