ID A0A1E3GUG2_9GAMM Unreviewed; 448 AA.
AC A0A1E3GUG2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=malate dehydrogenase (quinone) {ECO:0000256|ARBA:ARBA00013026};
DE EC=1.1.5.4 {ECO:0000256|ARBA:ARBA00013026};
DE AltName: Full=MQO {ECO:0000256|ARBA:ARBA00031550};
DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000256|ARBA:ARBA00030660};
GN Name=mqo {ECO:0000313|EMBL:ODN67690.1};
GN ORFNames=A9E74_00520 {ECO:0000313|EMBL:ODN67690.1};
OS Methylophaga muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN67690.1, ECO:0000313|Proteomes:UP000094379};
RN [1] {ECO:0000313|EMBL:ODN67690.1, ECO:0000313|Proteomes:UP000094379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bur 1 {ECO:0000313|EMBL:ODN67690.1,
RC ECO:0000313|Proteomes:UP000094379};
RA Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA Mustakhimov I., Trotsenko Y.A.;
RT "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + a quinone = a quinol + oxaloacetate;
CC Xref=Rhea:RHEA:46012, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001139};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC oxaloacetate from (S)-malate (quinone route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005012}.
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:ODN67690.1}.
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DR EMBL; MCRI01000003; ODN67690.1; -; Genomic_DNA.
DR RefSeq; WP_069295089.1; NZ_MCRI01000003.1.
DR AlphaFoldDB; A0A1E3GUG2; -.
DR STRING; 291169.A9E74_00520; -.
DR PATRIC; fig|291169.3.peg.527; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000094379; Unassembled WGS sequence.
DR GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ODN67690.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094379}.
SQ SEQUENCE 448 AA; 50006 MW; 7D1D07017006012C CRC64;
MTDQIHQVAI IGGGVCGTAL LYMLAEYTDI NDIVLLEKYA GVARVNSHGR NNSQTIHCGD
IETNYTLEKA TKVKAAAEML VNFAAELPNV DQVIFKYPKM VLGVGDQECR QLRQRYQTFR
EVFPNMQLLE KSDIASHEPA VVMINGEMRP EPCVALAVLD DYSAVDYQRL SEAFVDKAKA
KTDKQIQLLF NSEVDDIVEK DGVFSLVTGD KIIKARSVVV SAGGHSLLLA QKMGYGLEFS
CLPVAGSFYF TPQVLRGKVY TVQNDALPFA AVHGDPDVLI EGKTRFGPTA LLLPLLERYN
NKTFFEFLRV LRLDSRVMKV FWDLFRIKDI RNYIFKNFLF EVPLLRRWLF LKDARKIVPG
LQLKDIEFAK GFGGVRPQLI DKKNAKLLMG EAKINPGTGI VFNMTPSPGG TSCLENAETD
MRIIASRLGA TINEAVLNDT LHKTATLN
//