MMAB_BOVIN
ID MMAB_BOVIN Reviewed; 241 AA.
AC Q58D49; Q2NL20;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Corrinoid adenosyltransferase MMAB {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:12514191};
DE AltName: Full=ATP:co(I)rrinoid adenosyltransferase MMAB;
DE AltName: Full=Methylmalonic aciduria type B homolog;
DE Flags: Precursor;
GN Name=MMAB {ECO:0000250|UniProtKB:Q96EY8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12514191; DOI=10.1074/jbc.m212739200;
RA Leal N.A., Park S.D., Kima P.E., Bobik T.A.;
RT "Identification of the human and bovine ATP:Cob(I)alamin
RT adenosyltransferase cDNAs based on complementation of a bacterial mutant.";
RL J. Biol. Chem. 278:9227-9234(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 (PubMed:12514191). Generates adenosylcobalamin (AdoCbl) and directly
CC delivers the cofactor to MUT in a transfer that is stimulated by ATP-
CC binding to MMAB and gated by MMAA (By similarity).
CC {ECO:0000250|UniProtKB:Q96EY8, ECO:0000269|PubMed:12514191}.
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:0000269|PubMed:12514191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56797;
CC Evidence={ECO:0000305|PubMed:12514191};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q96EY8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96EY8}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BT021748; AAX46595.1; -; mRNA.
DR EMBL; BC111194; AAI11195.1; -; mRNA.
DR RefSeq; NP_001073100.1; NM_001079632.1.
DR AlphaFoldDB; Q58D49; -.
DR SMR; Q58D49; -.
DR STRING; 9913.ENSBTAP00000006821; -.
DR PRIDE; Q58D49; -.
DR GeneID; 617636; -.
DR KEGG; bta:617636; -.
DR CTD; 326625; -.
DR eggNOG; ENOG502QS64; Eukaryota.
DR InParanoid; Q58D49; -.
DR OrthoDB; 788789at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; IDA: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; ATP-binding; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..241
FT /note="Corrinoid adenosyltransferase MMAB"
FT /id="PRO_0000238932"
FT REGION 27..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..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:0000250|UniProtKB:Q9D273"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D273"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D273"
FT CONFLICT 25
FT /note="R -> S (in Ref. 3; AAI11195)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> V (in Ref. 3; AAI11195)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="H -> Q (in Ref. 3; AAI11195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 26587 MW; 7599729A1AFF48A9 CRC64;
MAVWGPGGRL GLRGCLGARK LLCPRFQSRG PQGVEDGDRP QPSSKTPKVP KIYTKTGDKG
FSSTFTGERR SKDDQVFEAV GTTDELSSAI GFAMELIAEK GHPFVEELQK IQCSLQDVGS
ALATPRSSAR EAHLKHATFE AGPILELEQW IDKYSRQLPP LTAFILPSGG KSSSALHFCR
AVCRRAERRV VPLVQTGETD ANVVKFLNRL SDYLFTLARY TAMKEGNPEK IYKKNDLSDR
T
