MMAB

Protein-coding gene in the species Homo sapiens

For other uses, see MMAB (disambiguation).

MMAB

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

2IDX

Identifiers
Aliases| MMAB, ATR, CFAP23, cblB, cob, methylmalonic aciduria (cobalamin deficiency) cblB type, metabolism of cobalamin associated B
External IDs| OMIM: 607568; MGI: 1924947; HomoloGene: 12680; GeneCards: MMAB; OMA:MMAB - orthologs
| Gene location (Human)

Chr.| Chromosome 12 (human)[1]

Band| 12q24.11| Start| 109,553,715 bp[1]
End| 109,573,580 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 5 (mouse)[2]

Band| 5|5 F| Start| 114,569,095 bp[2]
End| 114,582,121 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* right lobe of liver

* right adrenal cortex

* left adrenal gland

* left adrenal cortex

* apex of heart

* C1 segment

* pancreatic ductal cell

* mucosa of transverse colon

* right auricle of heart

* olfactory zone of nasal mucosa

| Top expressed in

* lumbar spinal ganglion

* muscle of thigh

* interventricular septum

* otic vesicle

* neural layer of retina

* saccule

* right kidney

* ascending aorta

* myocardium of ventricle

* neural tube

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* transferase activity
* nucleotide binding
* cob(I)yrinic acid a,c-diamide adenosyltransferase activity
* ATP binding
* protein binding
* cobalamin binding

Cellular component|

* mitochondrial matrix
* mitochondrion

Biological process|

* cobalamin metabolic process
* cobalamin biosynthetic process

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

326625

77697

Ensembl| |

ENSG00000139428

ENSMUSG00000029575

UniProt| |

Q96EY8

Q9D273

RefSeq (mRNA)| |

NM_052845

NM_029956
NM_001347398

RefSeq (protein)| |

NP_443077

NP_001334327
NP_084232

Location (UCSC)| Chr 12: 109.55 – 109.57 Mb| Chr 5: 114.57 – 114.58 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial is an enzyme that in humans is encoded by the MMAB gene.[5][6][7]

## Function

[edit]

This gene encodes an enzyme (cob(I)yrinic acid a,c-diamide adenosyltransferase) that catalyzes the final step in the conversion of vitamin B12 into adenosylcobalamin (AdoCbl), a vitamin B12-containing coenzyme for methylmalonyl-CoA mutase.[7]

## Clinical significance

[edit]

Mutations in the gene are the cause of vitamin B12-dependent methylmalonic aciduria linked to the cblB complementation group.[7]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000139428 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029575 - Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Dobson CM, Wai T, Leclerc D, Kadir H, Narang M, Lerner-Ellis JP, et al. (December 2002). "Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria". Human Molecular Genetics. 11 (26): 3361–3369\. doi:10.1093/hmg/11.26.3361. PMID 12471062.
6. ^ Leal NA, Park SD, Kima PE, Bobik TA (March 2003). "Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant". The Journal of Biological Chemistry. 278 (11): 9227–9234\. doi:10.1074/jbc.M212739200. PMID 12514191.
7. ^ a b c "Entrez Gene: MMAB methylmalonic aciduria (cobalamin deficiency) cblB type".

## External links

[edit]

* GeneReviews/NCBI/NIH/UW entry on Methylmalonic Acidemia
* PDBe-KB provides an overview of all the structure information available in the PDB for Human Corrinoid adenosyltransferase (MMAB)

## Further reading

[edit]

* Willer CJ, Sanna S, Jackson AU, Scuteri A, Bonnycastle LL, Clarke R, et al. (February 2008). "Newly identified loci that influence lipid concentrations and risk of coronary artery disease". Nature Genetics. 40 (2): 161–169\. doi:10.1038/ng.76. PMC 5206900. PMID 18193043.
* Hörster F, Baumgartner MR, Viardot C, Suormala T, Burgard P, Fowler B, et al. (August 2007). "Long-term outcome in methylmalonic acidurias is influenced by the underlying defect (mut0, mut-, cblA, cblB)". Pediatric Research. 62 (2): 225–230\. doi:10.1203/PDR.0b013e3180a0325f. PMID 17597648.
* Keeratichamroen S, Cairns JR, Sawangareetrakul P, Liammongkolkul S, Champattanachai V, Srisomsap C, et al. (June 2007). "Novel mutations found in two genes of thai patients with isolated methylmalonic acidemia". Biochemical Genetics. 45 (5–6): 421–430\. CiteSeerX 10.1.1.509.517. doi:10.1007/s10528-007-9085-y. PMID 17410422. S2CID 20799098.5–6&rft.pages=421-430&rft.date=2007-06&rft_id=https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.509.517#id-name=CiteSeerX&rft_id=https://api.semanticscholar.org/CorpusID:20799098#id-name=S2CID&rft_id=info:pmid/17410422&rft_id=info:doi/10.1007/s10528-007-9085-y&rft.aulast=Keeratichamroen&rft.aufirst=S&rft.au=Cairns,+JR&rft.au=Sawangareetrakul,+P&rft.au=Liammongkolkul,+S&rft.au=Champattanachai,+V&rft.au=Srisomsap,+C&rft.au=Kamolsilp,+M&rft.au=Wasant,+P&rft.au=Svasti,+J&rfr_id=info:sid/en.wikipedia.org:MMAB" class="Z3988">
* Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65\. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
* Martínez MA, Rincón A, Desviat LR, Merinero B, Ugarte M, Pérez B (April 2005). "Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants". Molecular Genetics and Metabolism. 84 (4): 317–325\. doi:10.1016/j.ymgme.2004.11.011. PMID 15781192.
* Leal NA, Olteanu H, Banerjee R, Bobik TA (November 2004). "Human ATP:Cob(I)alamin adenosyltransferase and its interaction with methionine synthase reductase". The Journal of Biological Chemistry. 279 (46): 47536–47542\. doi:10.1074/jbc.M405449200. PMID 15347655.
* Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (September 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50\. doi:10.1006/geno.1994.1457. hdl:10669/15162. PMID 7829101.

* v
* t
* e

PDB gallery

* 2idx: Structure of Human ATP:Cobalamin adenosyltransferase bound to ATP.

* v
* t
* e

Metabolism of vitamins, coenzymes, and cofactors

Fat soluble vitamins|

| Vitamin A|

* Retinol binding protein

|

Vitamin E|

* Alpha-tocopherol transfer protein

Vitamin D|

* liver (Sterol 27-hydroxylase or CYP27A1)
* renal (25-Hydroxyvitamin D3 1-alpha-hydroxylase or CYP27B1)
* degradation (1,25-Dihydroxyvitamin D3 24-hydroxylase or CYP24A1)

Vitamin K|

* Vitamin K epoxide reductase

Water soluble vitamins|

| Thiamine (B1)|

* Thiamine diphosphokinase

|

Niacin (B3)|

* Indoleamine 2,3-dioxygenase
* Formamidase

Pantothenic acid (B5)|

* Pantothenate kinase

Folic acid (B9)|

* Dihydropteroate synthase
* Dihydrofolate reductase
* Serine hydroxymethyltransferase

* Methylenetetrahydrofolate reductase

Vitamin B12|

* MMAA
* MMAB
* MMACHC
* MMADHC

Vitamin C|

* L-gulonolactone oxidase

Riboflavin (B2)|

* Riboflavin kinase

Nonvitamin cofactors|

| Tetrahydrobiopterin|

* GTP cyclohydrolase I
* 6-pyruvoyltetrahydropterin synthase
* Sepiapterin reductase

* PCBD1
* PTS
* QDPR

Molybdopterin|

* MOCS1
* MOCS2
* MOCS3
* Gephyrin

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