ID A0A1G6HBK7_9ACTN Unreviewed; 515 AA.
AC A0A1G6HBK7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=GA0111570_10898 {ECO:0000313|EMBL:SDB91672.1};
OS Raineyella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Raineyella.
OX NCBI_TaxID=1577474 {ECO:0000313|EMBL:SDB91672.1, ECO:0000313|Proteomes:UP000199086};
RN [1] {ECO:0000313|EMBL:SDB91672.1, ECO:0000313|Proteomes:UP000199086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ-22 {ECO:0000313|EMBL:SDB91672.1,
RC ECO:0000313|Proteomes:UP000199086};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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; FMYF01000008; SDB91672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6HBK7; -.
DR STRING; 1577474.GA0111570_10898; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000199086; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00212}; Reference proteome {ECO:0000313|Proteomes:UP000199086};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 515 AA; 57338 MW; C427F2FD2CCA5674 CRC64;
MAFDKRKPSK WPVEAQEVDV ALIGGGVLSA TFGLMLHMLQ PDWTIMGFER LPKVAKESSN
PWNNAGTGHA GLCELNYTKE KSDGTMDNSK PIDINEQFQV SRQLWAHFVE TGVLGHPETF
INPTPHMSLV HGDQDVDFLR RRWEGLKENP LFAAMEFSDD QEKIKEWAPL IVQGRDPKEH
IAVTYDPTGT DVNFGSVTRQ MFNYLEYHGV FVETSKEVTD LKQNSDGSWT LRVADHRRRD
EGRGPDKFVR AKFVFNGAGG WALKMLQKAG IPEVEGYALF PVSGAFLNTT DPTIVNTHKV
KVYGKAKVGA PPMSNPHMDA RIINTNRSVL FGPYAGVDPR FLKYGSLLDL PKMIRTHNLL
AVLNVGRENI PLIKMLAGMI FMTPRQKLNE LRDFAPDAHI TDWRMIKAGQ RAQIIKTNAE
GHGKLEFGTE VITSNDGTLA AVLGASPGAS TAVPIMLELL ERCFPEQIEG WRPKIKEVIP
TYGEKLSDDP AKAYEVMTHT AKVLNLTPPA KPDGV
//
