GenomeNet

Database: UniProt
Entry: A0A0A8HLT8_STAHY
LinkDB: A0A0A8HLT8_STAHY
Original site: A0A0A8HLT8_STAHY 
ID   A0A0A8HLT8_STAHY        Unreviewed;       497 AA.
AC   A0A0A8HLT8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 55.
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   ECO:0000313|EMBL:RIO47270.1};
GN   ORFNames=BUZ57_01940 {ECO:0000313|EMBL:RIO47270.1}, GLV83_00140
GN   {ECO:0000313|EMBL:NJI30103.1};
OS   Staphylococcus hyicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1284 {ECO:0000313|EMBL:RIO47270.1, ECO:0000313|Proteomes:UP000285625};
RN   [1] {ECO:0000313|EMBL:RIO47270.1, ECO:0000313|Proteomes:UP000285625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SNUC 5959 {ECO:0000313|EMBL:RIO47270.1,
RC   ECO:0000313|Proteomes:UP000285625};
RX   PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA   Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA   De Buck J.;
RT   "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT   Species Based on Whole-Genome Sequencing.";
RL   Front. Microbiol. 7:1990-1990(2016).
RN   [2] {ECO:0000313|EMBL:NJI30103.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1380 {ECO:0000313|EMBL:NJI30103.1};
RA   Rhoads D., Shwani A., Adkins P., Calcutt M., Middleton J.;
RT   "Whole genome comparisons of Staphylococcus agnetis isolates from cattle
RT   and chickens.";
RL   Submitted (NOV-2019) 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:RIO47270.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; WMFP01000003; NJI30103.1; -; Genomic_DNA.
DR   EMBL; QXVO01000004; RIO47270.1; -; Genomic_DNA.
DR   RefSeq; WP_039643654.1; NZ_WMFP01000003.1.
DR   AlphaFoldDB; A0A0A8HLT8; -.
DR   STRING; 1284.SHYC_00875; -.
DR   GeneID; 41072029; -.
DR   KEGG; shu:SHYC_00875; -.
DR   HOGENOM; CLU_028151_0_0_9; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000285625; Unassembled WGS sequence.
DR   Proteomes; UP000606275; Unassembled WGS sequence.
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   NCBIfam; NF040844; Lac_Quin_Ox_NO; 1.
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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00212};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00212}.
SQ   SEQUENCE   497 AA;  56327 MW;  62C0A551C71289A2 CRC64;
     MSNQSEPRNI IVVGAGVLST TFSSMIKELE PNWNIKLYER LDRPGLESSN ERHNAGTGHA
     ALCELNYTVL QPDGSIDIEK AKHINEEFEI SKQFWGFLVK NKNISNPREF INPLPHISFV
     RGVNNRKFLK DRYEAMKQSP MFDNIEYTED IEVMRKWMPL MMKGRDASDI MAASKIDEGT
     DVNFGELTRK MTSNIEAHDN AEVKYNHEVI DFMQREDKKW EVKIRNRNSG KVFTEIAHHV
     FIGAGGGAIP LLQKTGIPES KNLGGFPITG QFLTCTNPEV VEEHGVKVYG KEPPGTPPMT
     VPHLDTRYIN GEKTLLFGPF ASVGPKFLKN GSNLDLFRSV KPYNIMTLLA SAAKNLPLIK
     YSFDQILMTK EGCMNHLRTF YPEARDEDWE LYTAGKRVQV IKDTEEYGKG FIQFGTEVVN
     SQDHTVIALL GESPGASTSV SVALEVLEKN FPELTSEWTP KIQKMIPSYG KSLIEDEALM
     RKTRKQTSKD LELNYYE
//
DBGET integrated database retrieval system