ID A0A0C1JK79_9RHOB Unreviewed; 757 AA.
AC A0A0C1JK79;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KIC43937.1};
GN ORFNames=RA28_13050 {ECO:0000313|EMBL:KIC43937.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC43937.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(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:KIC43937.1}.
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DR EMBL; JWLK01000005; KIC43937.1; -; Genomic_DNA.
DR RefSeq; WP_039529564.1; NZ_JWLK01000005.1.
DR AlphaFoldDB; A0A0C1JK79; -.
DR STRING; 1577904.RA28_13050; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000031326; 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:UP000031326}.
FT DOMAIN 20..153
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 165..402
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 78..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 757 AA; 82086 MW; 38C1624A95383E04 CRC64;
MSDTPSLRQA ALDYHAYPKP GKLEIKATKP MANGRDLARA YSPGVAEAST EIKADPTNAE
KYTSRGNLVA VVSNGTAVLG LGNIGALASK PVMEGKAVLF KKFAGIDCFD IEVDQPDPEK
LADIVCALEP TFGAINLEDI KAPDCFVVEK LCRERMNIPV FHDDQHGTAI VVGAAAKNAL
HVAGKKFEDI KIVSTGGGAA GIACLSMLEK LGVKRENIWL CDIHGLVYEG RQEDMNPHKD
QFAQKTDLRT LDDVIDGADL FLGLSGPNVL KPEMVERMAK RPIIFALANP TPEILPQAAR
EVVPDAIIAT GRSDFPNQVN NVLCFPFIFR GALDVGATEI NDEMQIACVD GIAEMARATT
SAEAAAAYKG EQLTFGPDYL IPKPFDPRLV GVVSSSVARA AMESGVAKRP IADLEAYKER
LNQTVFKSAL LMRPVFEAAA VASRRIVFAE GEDERVLRAA QAVLEETTET PILIGRPDVI
DARCERLGLT VKPGEDFQIV NPENDPRYYD YWNSYHQIMQ RKGVTPDLAK AIMRTNTTAI
GAIMVHRGEA DSMICGTFGE YRWHLNYVQQ IFDDGAMHPH GALSLMILED GPLFIADTHV
RQLPDPAELA ESTIGAARHV RRFGIEPKIA FCSQSQFGNQ AEGSGKRLRA AIDILDSEPR
DFVYEGEMNL DLALDPELRG RIFPNSRLEG PANVLIFAHA DAASGVRNIL KMKADGLEVG
PILMGMGNKA HIVTPSITAR GLLNMAAIAG TPVAHYG
//
