MMAA1_CAEEL
ID MMAA1_CAEEL Reviewed; 399 AA.
AC Q22111; Q6AHP0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
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; ORFNames=T02G5.13;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16843692; DOI=10.1016/j.ymgme.2006.06.001;
RA Chandler R.J., Aswani V., Tsai M.S., Falk M., Wehrli N., Stabler S.,
RA Allen R., Sedensky M., Kazazian H.H., Venditti C.P.;
RT "Propionyl-CoA and adenosylcobalamin metabolism in Caenorhabditis elegans:
RT evidence for a role of methylmalonyl-CoA epimerase in intermediary
RT metabolism.";
RL Mol. Genet. Metab. 89:64-73(2006).
CC -!- FUNCTION: May have GTPase activity. May also bind and hydrolyze ATP.
CC May function as chaperone (By similarity). Likely to have a role in
CC propionyl-CoA and adenosylcobalamin metabolism. {ECO:0000250,
CC ECO:0000269|PubMed:16843692}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q22111-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q22111-2; Sequence=VSP_039464;
CC -!- DISRUPTION PHENOTYPE: Reduced incorporation of 1-[14C]-propionate.
CC Defective in adenosylcobalamin synthesis. incorporation into
CC macromolecules. {ECO:0000269|PubMed:16843692}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000305}.
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DR EMBL; FO081112; CCD69185.1; -; Genomic_DNA.
DR EMBL; FO081112; CCD69186.1; -; Genomic_DNA.
DR PIR; T16792; T16792.
DR RefSeq; NP_001022302.1; NM_001027131.4. [Q22111-1]
DR RefSeq; NP_001022303.1; NM_001027132.3.
DR AlphaFoldDB; Q22111; -.
DR SMR; Q22111; -.
DR BioGRID; 39500; 9.
DR STRING; 6239.T02G5.13a; -.
DR EPD; Q22111; -.
DR PaxDb; Q22111; -.
DR PeptideAtlas; Q22111; -.
DR EnsemblMetazoa; T02G5.13a.1; T02G5.13a.1; WBGene00020169. [Q22111-1]
DR EnsemblMetazoa; T02G5.13b.1; T02G5.13b.1; WBGene00020169. [Q22111-2]
DR EnsemblMetazoa; T02G5.13b.2; T02G5.13b.2; WBGene00020169. [Q22111-2]
DR GeneID; 174164; -.
DR KEGG; cel:CELE_T02G5.13; -.
DR UCSC; T02G5.13a; c. elegans.
DR CTD; 174164; -.
DR WormBase; T02G5.13a; CE31822; WBGene00020169; mmaa-1. [Q22111-1]
DR WormBase; T02G5.13b; CE04865; WBGene00020169; mmaa-1. [Q22111-2]
DR eggNOG; ENOG502QR2W; Eukaryota.
DR GeneTree; ENSGT00390000009908; -.
DR InParanoid; Q22111; -.
DR OMA; WMWERID; -.
DR OrthoDB; 817699at2759; -.
DR PhylomeDB; Q22111; -.
DR Reactome; R-CEL-71032; Propionyl-CoA catabolism.
DR Reactome; R-CEL-9759218; Cobalamin (Cbl) metabolism.
DR PRO; PR:Q22111; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020169; Expressed in germ line (C elegans) and 4 other tissues.
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 Alternative splicing; ATP-binding; Chaperone; GTP-binding; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..399
FT /note="Methylmalonic aciduria type A homolog,
FT mitochondrial"
FT /id="PRO_0000157821"
FT BINDING 131..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 310..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_039464"
SQ SEQUENCE 399 AA; 44216 MW; D3F27A79C38F3697 CRC64;
MVVRSLLRVS RLTSASCRHA SLAVSSTPKP YIPSVTGVQK SMPFDNLLEQ YSRVHWDDSV
TYDDPNVQKL FKSLMSGSRA ALASAITLVE SRHPTKRAQG NMLLKMVLDE EREKYKKFGR
DSMIFRVGIS GSPGVGKSSF IEALGAELTE NRGKKVAVLT IDPTSAMTGG SVLGDLTRMQ
ELSRNPKAYI RQSPTSGSLG GVTRGIHEAV ILCEGAGYDI VIIETVGVGQ SETSVSDMCD
MMCLLLSPAH GDELQGVKRG IMEMSDLLVV TKDDGDLKAK AKMTQAEYIS ALKFMRPRLD
VWRPKVMRSS IMDKESVSEV CSSLYEFWDT IGESGDLERR RQDQMKKWMW NHVKDEIMSV
FQKHPKIAHL APKLENEIRS GKITPGLAAE TMIRTFFGV
