P80078 (MAMA_CLOCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylaspartate mutase S chain
EC=5.4.99.1

Alternative name(s):
Glutamate mutase subunit sigma

Gene names

Name:	mamA
Synonyms:	glmS

Organism

Clostridium cochlearium

Taxonomic identifier

1494 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-threo-3-methylaspartate = L-glutamate. HAMAP-Rule MF_00526
Cofactor	5'-deoxy-5'-adenosyl-adeninylcobamide (pseudo-coenzyme B12).
Pathway	Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. HAMAP-Rule MF_00526
Subunit structure	Heterotetramer of 2 E subunits and 2 S subunits.
Sequence similarities	Contains 1 B12-binding domain.

Ontologies

Keywords
Ligand	Cobalamin Cobalt Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	anaerobic glutamate catabolic process Inferred from electronic annotation. Source: HAMAP glutamate catabolic process via L-citramalate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylaspartate mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
glmE	P80077	2	EBI-1028147,EBI-1028142

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 137

137

Methylaspartate mutase S chain HAMAP-Rule MF_00526

PRO_0000216443

Regions

Domain

3 – 137

135

B12-binding

Sites

Metal binding

16

1

Cobalt (cobalamin axial ligand)

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

137

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

18 – 29

12

Beta strand

33 – 41

9

Helix

43 – 53

11

Beta strand

56 – 62

7

Helix

67 – 71

5

Helix

74 – 80

7

Beta strand

87 – 93

7

Beta strand

95 – 98

4

Helix

101 – 110

10

Beta strand

114 – 116

3

Helix

123 – 134

12

Sequences

	Sequence		Length	Mass (Da)
	P80078 [UniParc]. Last modified December 13, 2001. Version 2. Checksum: D9C5BF8DE5D1E878	FASTA	137	14,812
	10 20 30 40 50 60 MEKKTIVLGV IGSDCHAVGN KILDHAFTNA GFNVVNIGVL SPQEVFIKAA IETKADAILL 70 80 90 100 110 120 SSLYGQGEID CKGLRQKCDE AGLEGILLYV GGNIVVGKQH WPDVEKRFKD MGYDRVYAPG 130 TPPEVGIADL KKDLNIE

References

[1]	"Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli." Zelder O., Beatrix B., Leutbecher U., Buckel W. Eur. J. Biochem. 226:577-585(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[2]	"Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium." Zelder O., Beatrix B., Buckel W. FEMS Microbiol. Lett. 118:15-21(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[3]	"Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors." Leutbecher U., Boecher R., Linder D., Buckel W. Eur. J. Biochem. 205:759-765(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-23. Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[4]	"Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights." Reitzer R., Gruber K., Jogl G., Wagner U.G., Bothe H., Buckel W., Kratky C. Structure 7:891-902(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X80997 Genomic DNA. Translation: CAA56921.1.
X75890 Genomic DNA. Translation: CAA53484.1.

PIR

I40658.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B1A	NMR	-	A	1-137	[»]
1CB7	X-ray	2.00	A/C	1-137	[»]
1CCW	X-ray	1.60	A/C	1-137	[»]
1I9C	X-ray	1.90	A/C	1-137	[»]

ProteinModelPortal

P80078.

SMR

P80078. Positions 1-137.

ModBase

Search...

Protein-protein interaction databases

IntAct

P80078. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P80078.

UniPathway

UPA00561; UER00617.

Family and domain databases

Gene3D

3.40.50.280. 1 hit.

HAMAP

MF_00526. MthylAspMutase_S.

InterPro

IPR006158. Cobalamin-bd.
IPR006394. Me_Asp_mutase.
[Graphical view]

Pfam

PF02310. B12-binding. 1 hit.
[Graphical view]

SUPFAM

SSF52242. Cbl-bd. 1 hit.

TIGRFAMs

TIGR01501. MthylAspMutase. 1 hit.

PROSITE

PS51332. B12_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80078.

Entry information

Entry name

MAMA_CLOCO

Accession

Primary (citable) accession number: P80078
Secondary accession number(s): Q60144

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	December 13, 2001
Last modified:	April 3, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program