ID B8Y5H6_KLEPN Unreviewed; 151 AA.
AC B8Y5H6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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};
DE Flags: Fragment;
GN Name=mdh {ECO:0000313|EMBL:ACL13874.1};
OS Klebsiella pneumoniae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573 {ECO:0000313|EMBL:ACL13874.1};
RN [1] {ECO:0000313|EMBL:ACL13874.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cas120 {ECO:0000313|EMBL:ACL13890.1}, Cas121
RC {ECO:0000313|EMBL:ACL13891.1}, Sp22 {ECO:0000313|EMBL:ACL13882.1}, Sp3
RC {ECO:0000313|EMBL:ACL13874.1}, Sp34 {ECO:0000313|EMBL:ACL13886.1}, and
RC Sp41 {ECO:0000313|EMBL:ACL13888.1};
RX PubMed=19151141; DOI=10.1128/JB.00601-08;
RA Stahlhut S.G., Chattopadhyay S., Struve C., Weissman S.J., Aprikian P.,
RA Libby S.J., Fang F.C., Krogfelt K.A., Sokurenko E.V.;
RT "Population variability of the FimH type 1 fimbrial adhesin in Klebsiella
RT pneumoniae.";
RL J. Bacteriol. 191:1941-1950(2009).
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|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; FJ483653; ACL13874.1; -; Genomic_DNA.
DR EMBL; FJ483661; ACL13882.1; -; Genomic_DNA.
DR EMBL; FJ483665; ACL13886.1; -; Genomic_DNA.
DR EMBL; FJ483667; ACL13888.1; -; Genomic_DNA.
DR EMBL; FJ483669; ACL13890.1; -; Genomic_DNA.
DR EMBL; FJ483670; ACL13891.1; -; Genomic_DNA.
DR AlphaFoldDB; B8Y5H6; -.
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 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; 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; IPR036291; NAD(P)-bd_dom_sf.
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 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|RuleBase:RU000422};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU000422}.
FT DOMAIN 1..68
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 70..151
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACL13874.1"
FT NON_TER 151
FT /evidence="ECO:0000313|EMBL:ACL13874.1"
SQ SEQUENCE 151 AA; 15618 MW; 88FEFDFC0ACA3514 CRC64;
GVARKPGMDR SDLFNVNAGI VKNLVQQIAK TCPQACIGVI TNPVNTTVAI AAEVLKKAGV
YDKNKLFGVT TLDIIRSNTF VAELKGKSAT EVEVPVIGGH SGVTILPLLS QIPGVSFSDQ
EVADLTKRIQ NAGTEVVEAK AGGGSATLSM G
//
