MMAB_MOUSE
ID MMAB_MOUSE Reviewed; 237 AA.
AC Q9D273; Q3UFL6; Q8CBZ0; Q8VBZ4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Corrinoid adenosyltransferase MMAB {ECO:0000305};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:Q96EY8};
DE AltName: Full=ATP:co(I)rrinoid adenosyltransferase MMAB;
DE AltName: Full=Methylmalonic aciduria type B homolog;
DE Flags: Precursor;
GN Name=Mmab {ECO:0000312|MGI:MGI:1924947};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Diencephalon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-205 AND LYS-224, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Converts cob(I)alamin to adenosylcobalamin
CC (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase,
CC therefore participates in the final step of the vitamin B12 conversion.
CC Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor
CC to MUT in a transfer that is stimulated by ATP-binding to MMAB and
CC gated by MMAA. {ECO:0000250|UniProtKB:Q96EY8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cob(I)alamin-[corrinoid adenosyltransferase] =
CC adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] +
CC triphosphate; Xref=Rhea:RHEA:56796, Rhea:RHEA-COMP:14743, Rhea:RHEA-
CC COMP:14744, ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60488, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000250|UniProtKB:Q96EY8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56797;
CC Evidence={ECO:0000250|UniProtKB:Q96EY8};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q96EY8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96EY8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D273-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D273-2; Sequence=VSP_008847;
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK020286; BAB32055.1; -; mRNA.
DR EMBL; AK034288; BAC28659.1; -; mRNA.
DR EMBL; AK088785; BAC40571.1; -; mRNA.
DR EMBL; AK148421; BAE28544.1; -; mRNA.
DR EMBL; BC022159; AAH22159.1; -; mRNA.
DR EMBL; BC057558; AAH57558.1; -; mRNA.
DR CCDS; CCDS19565.1; -. [Q9D273-1]
DR RefSeq; NP_084232.1; NM_029956.3. [Q9D273-1]
DR AlphaFoldDB; Q9D273; -.
DR SMR; Q9D273; -.
DR BioGRID; 218853; 3.
DR IntAct; Q9D273; 1.
DR STRING; 10090.ENSMUSP00000031560; -.
DR iPTMnet; Q9D273; -.
DR PhosphoSitePlus; Q9D273; -.
DR EPD; Q9D273; -.
DR MaxQB; Q9D273; -.
DR PaxDb; Q9D273; -.
DR PeptideAtlas; Q9D273; -.
DR PRIDE; Q9D273; -.
DR ProteomicsDB; 295958; -. [Q9D273-1]
DR ProteomicsDB; 295959; -. [Q9D273-2]
DR Antibodypedia; 30891; 193 antibodies from 27 providers.
DR DNASU; 77697; -.
DR Ensembl; ENSMUST00000031560; ENSMUSP00000031560; ENSMUSG00000029575. [Q9D273-1]
DR Ensembl; ENSMUST00000123256; ENSMUSP00000142979; ENSMUSG00000029575. [Q9D273-2]
DR GeneID; 77697; -.
DR KEGG; mmu:77697; -.
DR UCSC; uc008yzo.1; mouse. [Q9D273-1]
DR UCSC; uc008yzp.1; mouse. [Q9D273-2]
DR CTD; 326625; -.
DR MGI; MGI:1924947; Mmab.
DR VEuPathDB; HostDB:ENSMUSG00000029575; -.
DR eggNOG; ENOG502QS64; Eukaryota.
DR GeneTree; ENSGT00390000008432; -.
DR HOGENOM; CLU_083486_1_1_1; -.
DR InParanoid; Q9D273; -.
DR OMA; HQACTVV; -.
DR OrthoDB; 788789at2759; -.
DR PhylomeDB; Q9D273; -.
DR TreeFam; TF312942; -.
DR Reactome; R-MMU-9759218; Cobalamin (Cbl) metabolism.
DR BioGRID-ORCS; 77697; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9D273; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D273; protein.
DR Bgee; ENSMUSG00000029575; Expressed in lumbar dorsal root ganglion and 240 other tissues.
DR ExpressionAtlas; Q9D273; baseline and differential.
DR Genevisible; Q9D273; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; ISO:MGI.
DR GO; GO:0031419; F:cobalamin binding; ISS:UniProtKB.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; ISS:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; ISS:UniProtKB.
DR Gene3D; 1.20.1200.10; -; 1.
DR InterPro; IPR016030; CblAdoTrfase-like.
DR InterPro; IPR036451; CblAdoTrfase-like_sf.
DR InterPro; IPR029499; PduO-typ.
DR PANTHER; PTHR12213; PTHR12213; 1.
DR Pfam; PF01923; Cob_adeno_trans; 1.
DR SUPFAM; SSF89028; SSF89028; 1.
DR TIGRFAMs; TIGR00636; PduO_Nterm; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..237
FT /note="Corrinoid adenosyltransferase MMAB"
FT /id="PRO_0000005569"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 62..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 184..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY8"
FT MOD_RES 205
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 210..237
FT /note="LSDYLFTVARYAAMKEGSQEKIYKKHDV -> CLSGVWRVCLTTRPLPSSCI
FT LDCAVSPVALSHSEVRLCLGNKSQRRHT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008847"
SQ SEQUENCE 237 AA; 26273 MW; CB0408BC575FE8CB CRC64;
MAVWLFGGRL GLRGRLSACR LLCPRFQSRG PQGGEDGDRL QPSSTAAKIP KIYTKTGDKG
FSSTFTGERR PKDDQVFEAV GTTDELSSAI GFAMELVTEK GHMFAEELQK IQCMLQDVGS
ALATPRSSAR EAHLKHTAFQ EGPVLELERW IDKYSSQLPP LKAFILPSGG KSSSALHFCR
AVCRRAERRV VPLVQMGETD ANVAKFLNRL SDYLFTVARY AAMKEGSQEK IYKKHDV
