ID A0A157SIW5_9BORD Unreviewed; 574 AA.
AC A0A157SIW5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:SAI70398.1};
GN ORFNames=SAMEA3906486_03069 {ECO:0000313|EMBL:SAI70398.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI70398.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI70398.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI70398.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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}.
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DR EMBL; FKIF01000006; SAI70398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A157SIW5; -.
DR STRING; 288768.SAMEA3906486_03069; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000076848; 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 HAMAP; MF_00212; MQO; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01320; mal_quin_oxido; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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.
DR PROSITE; PS51318; TAT; 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}; Reference proteome {ECO:0000313|Proteomes:UP000076848};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 552..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 62788 MW; 571AB5BB819D7BED CRC64;
MASKPNADAK TRAASKHSFT RRHFLGTAAL GAGAVAIGYH ALSDDQYRAE KADRNVDVLL
IGGGIMSATL GTYLTELEPK WSLEIFERLD GVAQESSNGW NNAGTGHSAL CELNYTPMDV
DGNVQIAKAI EINEQFQVSR QFWSHQVRRG VLGQPREFIN STPHMNLVWG QENVDFMKKR
VAALQASPLF TGMELTTDPA RIAEWVPVMM EGRQSGQMLA ATRSPLGTDV NLGEITRQFY
SHLTGTSKLK LSTGHEVRSI TRNPDGTWRV SAFDMKDGSK IQTVDARFVF IGAGGAALPL
LQKSGIPEGR QYGGFPVGGA FLVTENPEIA QRHLAKVYGM AETGSPPMSV PHLDTRVLDG
KRVLLFGPFA TWSSKFLKEG SYFDLPASLT MSNLIPSMQV GVHEFGLVKY LAEQLSLSKE
EQMNELRRYM PEARDEDWRL WQAGQRVQII KNDPEKGGEL KLGTEIVMAK DRSIAALLGA
SPGGSTSPAI MLSLLQRAFP DQVKSAAWQD KLHQIIPSYG RKLNENPELL ATVWRDTEQA
LQLAIPSPSL SGVQAGAAAP RNPAPVPKVS DIQL
//
