ID A0A0S2K5D6_9GAMM Unreviewed; 313 AA.
AC A0A0S2K5D6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
GN ORFNames=C1E23_08755 {ECO:0000313|EMBL:RZQ53483.1}, C1E24_07290
GN {ECO:0000313|EMBL:TLX47543.1}, CWB73_09290
GN {ECO:0000313|EMBL:TMP81038.1}, PP2015_2765
GN {ECO:0000313|EMBL:ALO43252.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43252.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO43252.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43252.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TMP81038.1, ECO:0000313|Proteomes:UP000307362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1189 {ECO:0000313|EMBL:TMP81038.1,
RC ECO:0000313|Proteomes:UP000307362};
RA Paulsen S., Gram L.K.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000291338, ECO:0000313|Proteomes:UP000309186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3663 {ECO:0000313|EMBL:TLX47543.1,
RC ECO:0000313|Proteomes:UP000309186}, and S3898
RC {ECO:0000313|EMBL:RZQ53483.1, ECO:0000313|Proteomes:UP000291338};
RA Paulsen S., Gram L., Machado H.;
RT "Co-occurrence of chitin degradation, pigmentation and bioactivity in
RT marine Pseudoalteromonas.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000307362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1189 {ECO:0000313|Proteomes:UP000307362};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:TMP81038.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S1189 {ECO:0000313|EMBL:TMP81038.1};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00000774,
CC ECO:0000256|RuleBase:RU000422};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
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DR EMBL; CP013187; ALO43252.1; -; Genomic_DNA.
DR EMBL; PPSX01000025; RZQ53483.1; -; Genomic_DNA.
DR EMBL; PPSW01000011; TLX47543.1; -; Genomic_DNA.
DR EMBL; PNCM01000017; TMP81038.1; -; Genomic_DNA.
DR RefSeq; WP_058030924.1; NZ_PPSX01000025.1.
DR AlphaFoldDB; A0A0S2K5D6; -.
DR STRING; 161398.PP2015_2765; -.
DR KEGG; pphe:PP2015_2765; -.
DR PATRIC; fig|161398.10.peg.2825; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000061457; Chromosome I.
DR Proteomes; UP000291338; Unassembled WGS sequence.
DR Proteomes; UP000307362; Unassembled WGS sequence.
DR Proteomes; UP000309186; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU000422};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU000422}.
FT DOMAIN 1..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..309
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 313 AA; 32247 MW; C79873E06C8256F1 CRC64;
MKVAVLGAAG GIGQALSLLL KNGLPAGSEL SLYDVAPVVP GVAVDLSHIP TAVKVAGFGA
DDLDAALAGA DIVLIPAGMP RKPGMDRADL FNVNAGIIKT LAEGIVRNCP KALVGVITNP
VNGTVPIVAE VFKKAGTYEA SRVFGVTTLD VIRSEAFVAE LKGVDVSEVK VPVIGGHSGT
TILPLLSQVE GVEFTEEEVA ALTPRIQNAG TEVVNAKAGG GSATLSMGAA AARFCFSLVK
GLQGEQNVVD YAYVAVENGD AAYFAHPVRL GTNGVEEILS YGELSAFEEK AKNDMLETLN
KDIQEGIDFM AAQ
//
