B2FSQ8

PR
Gene name
mqo
Protein name
Probable malate:quinone oxidoreductase
Names
MQO, Malate dehydrogenase [quinone]
Species
Stenotrophomonas maltophilia (strain K279a)
KEGG Pathway
sml:Smlt1234
EC number
1.1.5.4: With a quinone or similar compound as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

497-562 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B2FSQ8

Entry ID Method Resolution Chain Position Source
AF-B2FSQ8-F1 Predicted AlphaFoldDB

No variants for B2FSQ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2FSQ8

No associated diseases with B2FSQ8

3 regional properties for B2FSQ8

Type Name Position InterPro Accession
domain Protein kinase domain 63 - 336 IPR000719
active_site Serine/threonine-protein kinase, active site 185 - 197 IPR008271
binding_site Protein kinase, ATP binding site 69 - 90 IPR017441

Functions

Description
EC Number 1.1.5.4 With a quinone or similar compound as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
malate dehydrogenase (menaquinone) activity Catalysis of the reaction: (S)-malate + a menaquinone = oxaloacetate + a menaquinol.
malate dehydrogenase (quinone) activity Catalysis of the reaction: (S)-malate + a quinone = oxaloacetate + a quinol.

1 GO annotations of biological process

Name Definition
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKFGKALLA LLVLLLLAAA LFLYWPLTQR SVPAASNDKP VDVVLVGAGI MSITLATYLQ
70 80 90 100 110 120
ELQPDWNIQV YERLDGVAGE SSDGWNNAGT GHSAFAELNY TPELPDGSIE TKRAVGIAES
130 140 150 160 170 180
FEVSRQFWSH QVKEGRLSQP SDFINPTPHM SFVWGDDNIA YLHKRQQALV KNPLFYGMQY
190 200 210 220 230 240
SEDPAQIKQW APLLMEGRDP KQKVAATWMP LGTDVNFGVI TRQLTAGLQR SPNFSLHLNH
250 260 270 280 290 300
EVSALRQNAD KSWNVTVKDL KAGTESTTHA RFVFIGAGGA ALKLLQMSGI PESKDYAGFP
310 320 330 340 350 360
VGGQFLAFQG QDVTSRHGVK AYGMAETGSP PMSVPHLDAR KLDGKPVVLF GPFALYSTKF
370 380 390 400 410 420
LKHGSWWDLY SSVNHNNVGP MLEVGKDNLD LVQYLMGQAR LNDADRQAEL VKYFPTAKPG
430 440 450 460 470 480
DWKLVTAGQR VQIIKRDPLK GPVLQFGTEI VTDKDHTLAA LLGASPGAST SPPIMLDLMA
490 500 510 520 530 540
KAFPDQMKAG WEARLREIVP SYGRKLNDSA ALVNEIRTLT SQTLHLPYLE VPVDANAASP
550 560
AAAAVPAAAK EKRNANEELQ AL