ID A0A1I5EF45_9SPHN Unreviewed; 579 AA.
AC A0A1I5EF45;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05428984_2258 {ECO:0000313|EMBL:SFO10075.1};
OS Sphingomonas sp. OK281.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1881067 {ECO:0000313|EMBL:SFO10075.1, ECO:0000313|Proteomes:UP000199378};
RN [1] {ECO:0000313|EMBL:SFO10075.1, ECO:0000313|Proteomes:UP000199378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK281 {ECO:0000313|EMBL:SFO10075.1,
RC ECO:0000313|Proteomes:UP000199378};
RA de Groot N.N.;
RL Submitted (OCT-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, 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}.
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DR EMBL; FOVZ01000002; SFO10075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5EF45; -.
DR STRING; 1881067.SAMN05428984_2258; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000199378; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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}; Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 62657 MW; 2750FEE72DC6ED27 CRC64;
MPKRKGMTMR RDANDDVNSP NLRTGVTRRN LLGSAIVAGG AAALPIAHAD AANTERTVDV
LLIGGGIMSA TLAVLLRELE PTWTIEMVER LDKVADESSN GWNNAGTGHS ALCELNYTPV
NKADGKVEIA KAVEINEQFQ VTRQFLSHQV DTGILANPRS FINSTPHMNL VWGDANVAFL
QKRHAALQAS PLFSGMEFTT DPKQISQWVP VMMEGRAPGT KLAATRSPLG TDCDWGEVTR
QYIASLAKQD NFTLTTGHEV RSLERETIGG KKARWRVTAR DMKTDEKQVI KARFVFAGAG
GGALPILQKS GIPEADDYAG FPVGGSFLVA DKPAITHRHL AKVYGKAAVG SPPMSVPHLD
TRFLDGKQAL LFGPFATFST KFLKEGSYFD LPASVTLDNF RPMLAVGWDD FDLVEYLAGQ
LIMSDSDRMD ALREYFPGAK DADWRLWQAG QRVQIIKRDP DKGGVLRLGT EIVASKDGSI
AALLGASPGA STAPSIMLNL LKKVFPNHLA TAGWQAKIRE IVPTYGVMLN ETPDVLAEHW
ASTADMLQLA IPSPTVGVAA GPRPAAMRVK PDRSPDLAL
//
