Descriptions

MeaB is an accessory GTPase protein involved in the assembly, protection, and reactivation of 5’-deoxyadenosyl cobalamin-dependent methylmalonyl-CoA mutase (MCM). MeaB's autoinhibition involves the switch II motif, which suppresses intrinsic GTPase activity by stabilizing the GDP-bound state and preventing assembly of the active site with MCM. The motif plays a crucial role in regulating nucleotide-sensitive conformational changes in switch III, which are essential for its chaperone function.

Autoinhibitory domains (AIDs)

Target domain

178-188 (Switch III motif)

Relief mechanism

Partner binding

Assay

Mutagenesis experiment, Structural analysis

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

5 structures for C5AP93

Entry ID Method Resolution Chain Position Source
4JYB X-ray 210 A A/B 1-329 PDB
4JYC X-ray 220 A A/B/C/D 1-329 PDB
4LC1 X-ray 180 A A/B 1-329 PDB
8DPB X-ray 272 A A/B 1-329 PDB
AF-C5AP93-F1 Predicted AlphaFoldDB

No variants for C5AP93

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5AP93

No associated diseases with C5AP93

No regional properties for C5AP93

Type Name Position InterPro Accession
No domain, repeats, and functional sites for C5AP93

Functions

Description
EC Number
Subcellular Localization
PANTHER Family PTHR23408 METHYLMALONYL-COA MUTASE
PANTHER Subfamily PTHR23408:SF3 METHYLMALONIC ACIDURIA TYPE A PROTEIN, MITOCHONDRIAL
PANTHER Protein Class mutase
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
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSATLPDMDT LRERLLAGDR AALARAITLA ESRRADHRAA VRDLIDAVLP QTGRAIRVGI
70 80 90 100 110 120
TGVPGVGKST TIDALGSLLT AAGHKVAVLA VDPSSTRTGG SILGDKTRMA RLAIDRNAFI
130 140 150 160 170 180
RPSPSSGTLG GVAAKTRETM LLCEAAGFDV ILVETVGVGQ SETAVADLTD FFLVLMLPGA
190 200 210 220 230 240
GDELQGIKKG ILELADMIAV NKADDGDGER RASAAASEYR AALHILTPPS ATWTPPVVTI
250 260 270 280 290 300
SGLHGKGLDS LWSRIEDHRS KLTATGEIAG KRREQDVKWM WALVHERLHQ RLVGSAEVRQ
310 320
ATAEAERAVA GGEHSPAAGA DAIATLIGL