B0YD89

PR
Gene name
mcsA
Protein name
2-methylcitrate synthase, mitochondrial
Names
Methylcitrate synthase, (2S,3S)-2-methylcitrate synthase, Citrate synthase 2
Species
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
KEGG Pathway
EC number
2.3.3.5: Acyl groups converted into alkyl groups on transfer
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-60 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for B0YD89

Entry ID Method Resolution Chain Position Source
6BOL X-ray 220 A A/B 29-465 PDB
6BOM X-ray 205 A A/B/C/D/E/F 29-465 PDB
6BON X-ray 235 A A/B 29-465 PDB
6BOO X-ray 260 A A/B/C/D 29-465 PDB
AF-B0YD89-F1 Predicted AlphaFoldDB

No variants for B0YD89

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0YD89

No associated diseases with B0YD89

7 regional properties for B0YD89

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 398 - 567 IPR000795
domain Small GTP-binding protein domain 401 - 556 IPR005225
domain Translation initiation factor IF-2, N-terminal 1 - 51 IPR006847-1
domain Translation initiation factor IF-2, N-terminal 323 - 373 IPR006847-2
domain Initiation factor 2 associated domain, bacterial 62 - 100 IPR013575
domain Translation initiation factor IF- 2, domain 3 674 - 788 IPR023115
domain Translation initiation factor IF-2, domain II 574 - 667 IPR044145

Functions

Description
EC Number 2.3.3.5 Acyl groups converted into alkyl groups on transfer
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

2 GO annotations of molecular function

Name Definition
2-methylcitrate synthase activity Catalysis of the reaction: H(2)O + oxaloacetate + propanoyl-CoA = (2R,3S)-2-methylcitrate + CoA + H(+).
citrate (Si)-synthase activity Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA, where the acetyl group is added to the si-face of oxaloacetate; acetyl-CoA thus provides the two carbon atoms of the pro-S carboxymethyl group.

2 GO annotations of biological process

Name Definition
propionate catabolic process, 2-methylcitrate cycle The chemical reactions and pathways resulting in the breakdown of propionate that occurs in the 2-methylcitrate cycle.
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
MAMTMRSTRH ASKLAQTARL ALTNSRRYST AEPDLKTALK AVIPAKRELF KQVKERSDEV
70 80 90 100 110 120
IGEVKVANVI GGMRGLKSML WEGSVLDPEE GIRFHGKTIK DCQKELPKGT SGTEMLPEAM
130 140 150 160 170 180
FWLLLTGQVP STNQVRAFSR ELAEQSHLPQ HILDLIKSFP RSMHPMTQLS IAVAALNTES
190 200 210 220 230 240
KFAKAYEKGL SKADYWEPTF DDSISLLAKI PRVAALVFRP DEVDQVGTQA LDASQDWSYN
250 260 270 280 290 300
FAELLGKGGK ENQDFHDLLR LYLALHGDHE GGNVSAHATH LVGSALSDPF LSYSAGLLGL
310 320 330 340 350 360
AGPLHGLAAQ EVLRWILAMQ DKIGTKFTDD DVRNYLWDTL KSGRVVPGYG HGVLRKPDPR
370 380 390 400 410 420
FQALMDFAAT RPDVLANPVF QLVKKNSEIA PAVLTEHGKT KNPHPNVDAA SGVLFYHYGF
430 440 450 460
QQPLYYTVTF GVSRALGPLV QLIWDRALGL PIERPKSINL LGLKK