MQO_SHIDS
ID MQO_SHIDS Reviewed; 548 AA.
AC Q32I11;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=SDY_0866;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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; CP000034; ABB61044.1; -; Genomic_DNA.
DR RefSeq; WP_000758085.1; NC_007606.1.
DR RefSeq; YP_402535.1; NC_007606.1.
DR AlphaFoldDB; Q32I11; -.
DR STRING; 300267.SDY_0866; -.
DR EnsemblBacteria; ABB61044; ABB61044; SDY_0866.
DR KEGG; sdy:SDY_0866; -.
DR PATRIC; fig|300267.13.peg.1000; -.
DR HOGENOM; CLU_028151_0_0_6; -.
DR OMA; PHLDTRW; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000002716; 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..548
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_1000023815"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60274 MW; 36940168A0F085CE CRC64;
MKKVTAMLFS MAVGLNAVSM AAKAKASEEQ ETDVLLIGGG IMSATLGTYL RELEPEWSMT
MVERLEGVAQ ESSNGWNNAG TGHSALMELN YTPQNADGSI SIEKAVAINE AFQISRQFWA
HQVERGVLRT PRSFINTVPH MSFVWGEDNV NFLRARYAAL QQSSLFRGMR YSEDHAQIKE
WAPLVMEGRD PQQKVAATRT EIGTDVNYGE ITRQLISSLQ KKSNFSLQLS SEVRALKRND
DNTWTVTVAD LKNGTAQNIR AKFVFIGAGG AALKLLQESG IPEAKDYAGF PVGGQFLVSE
NPDVVNHHLA KVYGKASVGA PPMSVPHIDT RVLDGKRVVL FGPFATFSTK FLKNGSLWDL
MSSTTTSNVM PMMHVGLDNF DLVKYLVSQV MLSEEDRFEA LKEYYPQAKK EDWRLWQAGQ
RVQIIKRDAD KGGVLRLGTE VVSDQQGTIA ALLGASPGAS TAAPIMLNLL EKVFGDRVSS
PQWQATLKAI VPSYGRKLNG DVAATERELQ YTSEVLGLKY DRPQAADSTP KPQLKPQPVQ
KEVADIAL
