ID   MQO_ACIBC               Reviewed;         546 AA.
AC   B2HV78;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=ACICU_00887;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC56199.1; -; Genomic_DNA.
DR   RefSeq; WP_000714073.1; NZ_CP031380.1.
DR   AlphaFoldDB; B2HV78; -.
DR   GeneID; 66398120; -.
DR   KEGG; abc:ACICU_00887; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000008839; 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   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; Tricarboxylic acid cycle.
FT   CHAIN           1..546
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000099863"
SQ   SEQUENCE   546 AA;  60435 MW;  2AA186835981B9E2 CRC64;
     MKKFLKYLLV LIILILIAGI VFLFRPIASK QVQTAKDEPV VDAVLVGGGI MSATLGTYFT
     ELEPNWQIRM FERLDQVAQE SSNGFNNAGT GHSGFMEMNY TEEKNGKMEI AKAEKVASQF
     EVAKQFWSYQ VKQGVLAEPK TFINPVPHIA FVWGDNVKFL EKRYAAMIQS PLFKGMKFTE
     DPAVIKQWAP LVMTDRDPTQ KVAATRMEVG SDVNYGSITK QLVNHLNQNP NFKLQTSTEV
     TGISQNDDKT WTVSFKNLKT GKTDHVKTRF VFIGAGGAAV KLLQLTGLPE AKQYAGFPVG
     GEFLITDNPA ITAQHTAKVY GRAELGAPPM SVPHIDTRYI DGKKYVLFGP FATYSNKFLK
     NGSQLDLLAS TNKSNVLPMT TVGLENLDLV KYLVSQVMMS DEDRLNELRK YYPDAKAEDW
     RLSQGGQRVQ IIKKEPGKPA TLQFGTEIFA SKDGAVTALL GASPGASTSP YIMLNLLEKA
     FPQQTEGKWN QKLHEIVVSY KQDLSKDPVL LDKVRQYTSS TLGLNYTSPF KAANDETAAA
     PVAKAN