MMAA1_CAEBR
ID MMAA1_CAEBR Reviewed; 412 AA.
AC A8XGZ9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Methylmalonic aciduria type A homolog, mitochondrial;
DE EC=3.6.-.-;
DE AltName: Full=Methylmalonic aciduria type A protein 1;
DE Flags: Precursor;
GN Name=mmaa-1 {ECO:0000312|EMBL:CAP31923.2}; ORFNames=CBG13064;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP31923.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP31923.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: May have GTPase activity. May also bind and hydrolyze ATP.
CC May function as chaperone. Likely to have a role in propionyl-CoA
CC metabolism and adenosylcobalamin synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000305}.
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DR EMBL; HE601401; CAP31923.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XGZ9; -.
DR SMR; A8XGZ9; -.
DR STRING; 6238.CBG13064; -.
DR WormBase; CBG13064; CBP40019; WBGene00033893; Cbr-mmaa-1.
DR eggNOG; ENOG502QR2W; Eukaryota.
DR HOGENOM; CLU_043725_2_2_1; -.
DR InParanoid; A8XGZ9; -.
DR OMA; WMWERID; -.
DR OrthoDB; 817699at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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.
DR TIGRFAMs; TIGR00750; lao; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; GTP-binding; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 16..412
FT /note="Methylmalonic aciduria type A homolog,
FT mitochondrial"
FT /id="PRO_0000395431"
FT BINDING 132..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 412 AA; 45794 MW; 34B55FEAA0FC9A15 CRC64;
MVVRALVRAH PLSRISCRYS SLAASSFNPK PYIPSVSGVQ KSLPFDNLLE QYSRVHWDDT
VTYDDPTVQR LFKNLMSGSR AALASAITLV ESRHPTKRAQ GNMLLKMVLD EEREKYKKYG
RDSMIFRVGI SGSPGVGKSS FIEALGAELT ENRGKKVAVL TIDPTSAMTG GSVLGDLTRM
QELSRNPRAY IRQSPTSGSL GGVTRGIHEA VILCEGAGYD IVIIETVGVG QSETSVSDMC
DMMCLLLSPA HGDELQGVKR GIMEMSDLLV VTKDDGDLQA KAKMTQAEYI SALKFMRPRL
DVWSPKVMRS SIMNKESVSA VCTSLYEFWD TIGESGDLER RRQDQMKKWM WNHVKDEIMA
VFQKHPKIIH LKNHKIFINL LLQAPKLEKD ISSGKITPGL AAETMIRTFF GV