MQO_GLUOX
ID MQO_GLUOX Reviewed; 500 AA.
AC Q5FP90;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00212};
DE EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=MQO {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00212};
GN Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=GOX2070;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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:0000255|HAMAP-Rule:MF_00212};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC oxaloacetate from (S)-malate (quinone route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00212}.
CC -!- SIMILARITY: Belongs to the MQO family. {ECO:0000255|HAMAP-
CC Rule:MF_00212}.
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DR EMBL; CP000009; AAW61806.1; -; Genomic_DNA.
DR RefSeq; WP_011253583.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FP90; -.
DR STRING; 290633.GOX2070; -.
DR EnsemblBacteria; AAW61806; AAW61806; GOX2070.
DR KEGG; gox:GOX2070; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_5; -.
DR OMA; RCDNPEV; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000006375; Chromosome.
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; -; 1.
DR HAMAP; MF_00212; MQO; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01320; mal_quin_oxido; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..500
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_1000023803"
SQ SEQUENCE 500 AA; 54100 MW; 2606F40BFFB27467 CRC64;
MPSLSSLCPD IVLIGAGIMS STLAALLREL DPSLSMVMFE TLSDCGQESS YAWNNAGTGH
AGNCELNYTP QRADGSVDIS KALAVNTEFD LSRQLWAHWV REGRIADPAA FVQPCPHISL
VWGAENVAFL KARYEAMVAH HCFADMEYTD DPAVIAQWAP LAMAGRDTTQ PVAATRIREG
TDVNFGALTH ALTASLKTDR SVSIHYNHRV TDLTRTEDGR WRVTATDTES GHAITVLTRF
VFIGAGGNAL PLLQKSGIPE ATHYAGFPVS GLWLRCTDPA ITRQHHAKVY GKAPVGSPPM
SVPHLDTRVI DGKSCLLFGP YAGFSTKFLK SGSWTDYFRS LTPKNIIPAL TAGKDNLGLL
DYLVKQVIQT NEARFQALLD FYPTARPEDW SKVVAGQRVQ IIRPDSGLHG KLRFGTELVK
NADRSLVAVL GASPGASIAA SVALQVVQGC FPERLVEGDW LPRLRQVFPA YGVDLTQDAA
ACATLRRDTA QVLGIASEAG