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Database: UniProt
Entry: N8XAN4_ACIBZ
LinkDB: N8XAN4_ACIBZ
Original site: N8XAN4_ACIBZ 
ID   N8XAN4_ACIBZ            Unreviewed;       547 AA.
AC   N8XAN4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=F963_02507 {ECO:0000313|EMBL:ENV21366.1};
OS   Acinetobacter bereziniae NIPH 3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217651 {ECO:0000313|EMBL:ENV21366.1, ECO:0000313|Proteomes:UP000013270};
RN   [1] {ECO:0000313|EMBL:ENV21366.1, ECO:0000313|Proteomes:UP000013270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 3 {ECO:0000313|EMBL:ENV21366.1,
RC   ECO:0000313|Proteomes:UP000013270};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter bereziniae NIPH 3.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENV21366.1}.
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DR   EMBL; APPK01000039; ENV21366.1; -; Genomic_DNA.
DR   RefSeq; WP_004831034.1; NZ_KB849468.1.
DR   AlphaFoldDB; N8XAN4; -.
DR   PATRIC; fig|1217651.3.peg.2466; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000013270; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   547 AA;  60442 MW;  7B939BC4F5FFA31B CRC64;
     MKRFFKYLLI VIGVVFVIGL IFLFRPISSK KVTTAADEPV VDVVLVGGGI MSATLGTYLN
     EVEPDWTVQM YERLDQVGQE SSAGFNNAGT GHSGFMEMNY TPEKDGKVDI KKAIDTASQF
     EVSKQFWSYQ VKNGVLGQPS SFINPVPHIA FVWGDSVNYM KKRYDAMRQS PMFEGLKYTE
     NPDEIKQWAP LVMQGRDANQ KVAATRMDVG SDVNYGSITT QLVDHLKKQP NFKLETSTEV
     TGISQNEDKT WTVSFKNLKT NQASHVKTRH VFIGAGGAAI RLLQMTGLEE TKQYAGFPIG
     GIFLMTDNPA VTAQHTAKVY GKPELGAPPM SVPHIDTRYV DGKKYVLFGP FATYSNKFLK
     NGSQFDLIDA TNKNNVIPMA TIGVENLDLV KYLVSQVAMS KQDQFNELKK YYPDAKIEDW
     NLSQAGQRVQ IIKKAPGKPA TLQFGTEIFS SKDGSITALL GASPGASTSP YIMLSLMEKA
     FPEQVKGKWN PKLHEIVKSY QQDLNSNPAL LDQVRTYTSA TLGLNYTPTR KAANDTTTAT
     PAVANAH
//
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