ID A0A0F4RKY5_9RHOB Unreviewed; 759 AA.
AC A0A0F4RKY5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KJZ20621.1};
GN ORFNames=TW80_07565 {ECO:0000313|EMBL:KJZ20621.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20621.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ20621.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ20621.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ20621.1}.
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DR EMBL; JXYE01000002; KJZ20621.1; -; Genomic_DNA.
DR RefSeq; WP_045996635.1; NZ_JXYE01000002.1.
DR AlphaFoldDB; A0A0F4RKY5; -.
DR STRING; 579483.TW80_07565; -.
DR PATRIC; fig|579483.3.peg.1549; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000033741; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
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; 81437 MW; 4A75A4C362C537C8 CRC64;
MTDDAKNSTR QAALDYHQFP KPGKLEIRAT KPLANGRDLS RAYSPGVAEA CVEIKANPDA
ARDYTTRGNL VGVVTNGTAV LGLGNIGGLA SKPVMEGKAV LFKKFANIDC FDIELNEPDP
EKLADIVCAL EPTFGAINLE DIKAPDCFIV EKICRERMNI PVFHDDQHGT AIVVGAAATN
ALRVAGKKFE DIKIVSTGGG AAGIACLNML LKLGVKRENV WLCDIEGLVY NGREKDMTPQ
KAEYAQGTTP ATLDDVIEGA DMFLGLSGPG VLKPEMVAKM SDAPIIFALA NPTPEISPDE
ARAVKADAII ATGRSDFPNQ VNNVLCFPFI FRGALDVGAT DINDEMKIAC IEGIAALARA
TTSAEAAAAY TGEKLTFGAD YLIPKPFDPR LMGVVASSVA KAAMETGIAT RPIEDMAAYK
ANLDGSVFKS AMIMRPVFEA ARTSSRSIVF AEGEDERVLR ASQAIMEETT DTPILIGRPD
VIAQRCERAG LKIRPGVDFS IVNPENDPRY RDYWETYHNL MARKGVTPDL AKAIMRTNTT
AIGAVMVHRG EADSLICGTF GQFRWHLKYV TQVLGNETLH PVGALSLMIL EDGPLFVADT
QVNAEPTPEQ IAETVIGAAR HVRRFGVEPK IALCSHSQFG NLDCDTGVRM RAAMAILDSE
PRDFAYEGEM HIDAALDVEL RNRVFPDAHL PGAANVLVFA NTDAASGVRN ILKMKGGGLE
VGPILMGMGN RCHIVTPSIT PRGLLNMSAL AGTPVAHYG
//
