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Database: UniProt
Entry: U2H6C0_9SPHI
LinkDB: U2H6C0_9SPHI
Original site: U2H6C0_9SPHI 
ID   U2H6C0_9SPHI            Unreviewed;       515 AA.
AC   U2H6C0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00212};
DE            EC=1.1.5.4 {ECO:0000256|HAMAP-Rule:MF_00212};
DE   AltName: Full=MQO {ECO:0000256|HAMAP-Rule:MF_00212};
DE   AltName: Full=Malate dehydrogenase [quinone] {ECO:0000256|HAMAP-Rule:MF_00212};
GN   Name=mqo {ECO:0000256|HAMAP-Rule:MF_00212};
GN   ORFNames=M472_00580 {ECO:0000313|EMBL:ERJ57251.1};
OS   Sphingobacterium paucimobilis HER1398.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ57251.1, ECO:0000313|Proteomes:UP000016584};
RN   [1] {ECO:0000313|EMBL:ERJ57251.1, ECO:0000313|Proteomes:UP000016584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HER1398 {ECO:0000313|EMBL:ERJ57251.1,
RC   ECO:0000313|Proteomes:UP000016584};
RX   PubMed=23929486;
RA   White R.A.III., Suttle C.A.;
RT   "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT   (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT   Member of the Genus Sphingobacterium (Bacteroidetes).";
RL   Genome Announc. 1:e00598-13(2013).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00212};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005012, ECO:0000256|HAMAP-Rule:MF_00212}.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000256|HAMAP-
CC       Rule:MF_00212}.
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:ERJ57251.1}.
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DR   EMBL; ATDL01000022; ERJ57251.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2H6C0; -.
DR   STRING; 1346330.M472_00580; -.
DR   PATRIC; fig|1346330.5.peg.3979; -.
DR   eggNOG; COG0579; Bacteria.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000016584; 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-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   HAMAP; MF_00212; MQO; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006231; MQO.
DR   NCBIfam; TIGR01320; mal_quin_oxido; 1.
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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00212};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00212};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00212}; Reference proteome {ECO:0000313|Proteomes:UP000016584};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ   SEQUENCE   515 AA;  57501 MW;  127BAC860A027617 CRC64;
     MIRNNEKRML ILQQFKEVMG KKKQNTEVDV VLIGGGIMSA TLGALINELN PDINIEIVER
     LDVVAAESSD AWNNAGTGHS ALCELNYTPE QADGSVKVEK AIKIAEQFEV SKQFWAYLVE
     KGVIQDPSHF IRQVPHMSAV FGEKDVRFLK TRFETMEKET LFKGMKYTED KSLLEQWIPL
     MMKDRAANEP MAATRMDIGT DVNFGALTKD LINYLRTKDN IKLSLHQEVK DIEREDDGRW
     EVEVKDLKTG EKRDIKAQFV FIGAGGHSLL LLEKSGIPEA KGYGGFPVGG QWLRCTNPEI
     IAQHRAKVYG KASVGAPPMS VPHLDTRYID GKQALLFGPY AGFSTKFLKQ GSYFDLPASI
     KLSNIKPMLS AGLDNLPLTK YLITEVMKKP KDKLDALKQF MPTARLEDWA IEKAGQRVQV
     IKKDPKHGGV LEFGTEVVSS ADGSIAALLG ASPGASTSVA IMIQLLKRCF PERAKSDEYR
     KKLREMIPSW GQSLNDNPEL CAEIRSHTHH VLQLD
//
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