ID   MMAA_RABIT              Reviewed;         413 AA.
AC   Q5MFW3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Methylmalonic aciduria type A homolog, mitochondrial {ECO:0000305};
DE            EC=3.6.-.- {ECO:0000250|UniProtKB:Q8IVH4};
DE   Flags: Precursor;
GN   Name=MMAA {ECO:0000250|UniProtKB:Q8IVH4};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yu W., Chen Q.;
RT   "Identification and analysis of stage-specific expression of MMAA gene
RT   during development of preimplantation rabbit nuclear transfer embryo.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase, binds and hydrolyzes GTP (By similarity). Involved in
CC       intracellular vitamin B12 metabolism, mediates the transport of
CC       cobalamin (Cbl) into mitochondria for the final steps of
CC       adenosylcobalamin (AdoCbl) synthesis (By similarity). Functions as a G-
CC       protein chaperone that assists AdoCbl cofactor delivery from MMAB to
CC       the methylmalonyl-CoA mutase (MMUT) (By similarity). Plays a dual role
CC       as both a protectase and a reactivase for MMUT (By similarity).
CC       Protects MMUT from progressive inactivation by oxidation by decreasing
CC       the rate of the formation of the oxidized inactive cofactor
CC       hydroxocobalamin (OH2Cbl) (By similarity). Additionally acts a
CC       reactivase by promoting the replacement of OH2Cbl by the active
CC       cofactor AdoCbl, restoring the activity of MMUT in the presence and
CC       hydrolysis of GTP (By similarity). {ECO:0000250|UniProtKB:Q8IVH4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:Q8IVH4};
CC   -!- ACTIVITY REGULATION: GTPase activity is stimulated by MMUT.
CC       {ECO:0000250|UniProtKB:Q8IVH4}.
CC   -!- SUBUNIT: Homodimer. Interacts with MMUT (the apoenzyme form); the
CC       interaction is GTP dependent. {ECO:0000250|UniProtKB:Q8IVH4}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8IVH4}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q8IVH4}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY830773; AAV88091.1; -; mRNA.
DR   RefSeq; NP_001076131.1; NM_001082662.1.
DR   AlphaFoldDB; Q5MFW3; -.
DR   SMR; Q5MFW3; -.
DR   GeneID; 100009376; -.
DR   KEGG; ocu:100009376; -.
DR   CTD; 166785; -.
DR   InParanoid; Q5MFW3; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005129; GTPase_ArgK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23408; PTHR23408; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; GTP-binding; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           66..413
FT                   /note="Methylmalonic aciduria type A homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000041877"
FT   REGION          362..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150..158
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVH4"
FT   BINDING         327..329
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVH4"
SQ   SEQUENCE   413 AA;  45682 MW;  84042932EFED2D13 CRC64;
     MAMLLPHPHP DFLKGLLKAP FRCYRFIFHS STHLGSGIPC AQPFNLLGLH YAKWMLLSDG
     LKRNLCVQTT LKDHKEGLSD KGQRFVDKLF TGLIQGQRAC LAEAKTLVES THSRKKELAQ
     VLLQKVLLFQ REQEQPNKGN PLAFRLGLSG PPGAGKSTFI EYSGKLLTER GHKLSVLAVG
     PSSCNSGGSL LGDKTRMTEF SRDMNAYIRP SPTRGNLGGV PRTTNEVILL CEGAGYDIIL
     IETVGVGQSE FAVADTVDIL FYYCHQLEEM NCRVSKEVYL RWQHGSNNYV CWRLDCASSK
     DTGRVCDALK LLRRRLAVWR PKVVRISARS WRGGHWNVGY DARILGPNTC QRGAACQTTK
     ATESLDVEPH SGKRVRAFQE SPHSPGADSC SGTKGPPWGP GPRASSRFVV EGF