Reviewed, UniProtKB/Swiss-Prot Q05488 (MAMA_CLOTT)

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:	mutS

Organism

Clostridium tetanomorphum

Taxonomic identifier

1553 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-threo-3-methylaspartate = L-glutamate. HAMAP MF_00526
Cofactor	5'-deoxy-5'-adenosyl-adeninylcobamide (pseudo-coenzyme B12). HAMAP MF_00526
Pathway	Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4. HAMAP MF_00526
Subunit structure	Heterotetramer of 2 E subunits and 2 S subunits. E exists as a homodimer and S as a monomer. HAMAP MF_00526
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
Molecular function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylaspartate mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 137

137

Methylaspartate mutase S chain HAMAP MF_00526

PRO_0000216445

Regions

Domain

3 – 137

135

B12-binding

Sites

Metal binding

16

1

Cobalt (cobalamin axial ligand) HAMAP MF_00526

Secondary structure

1

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137

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Beta strand

25 – 28

4

Turn

29 – 31

3

Beta strand

33 – 40

8

Helix

45 – 52

8

Beta strand

56 – 66

11

Helix

67 – 71

5

Helix

75 – 78

4

Beta strand

87 – 92

6

Beta strand

94 – 96

3

Helix

104 – 111

8

Beta strand

114 – 116

3

Turn

123 – 128

6

Helix

129 – 132

4

Sequences

	Sequence		Length	Mass (Da)
	Q05488-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E71FE55BA8CE3DB3	FASTA	137	14,748
	10 20 30 40 50 60 MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA IETKADLICV 70 80 90 100 110 120 SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN WPDVEQRFKA MGFDRVYPPG 130 TSPETTIADM KEVLGVE

References

[1]	"Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes." Marsh E.N.G., Holloway D.E. FEBS Lett. 310:167-170(1992) [PubMed: 1397267] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-33. Strain: NCIMB 11547.
[2]	"Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum." Brecht M., Kellermann J., Plueckthun A. FEBS Lett. 319:84-89(1993) [PubMed: 8454064] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-24. Strain: ATCC 15920 / DSM 528 / H1.
[3]	"How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum." Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B. Structure 6:1021-1033(1998) [PubMed: 9739092] [Abstract] Cited for: STRUCTURE BY NMR. Strain: ATCC 15920 / DSM 528 / H1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X70499 Genomic DNA. Translation: CAA49908.1.
X68570 Genomic DNA. Translation: CAA48567.1.

PIR

S29502.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BE1	NMR	-	A	1-137	[»]
1FMF	NMR	-	A	1-137	[»]
1ID8	NMR	-	A	1-137	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.4.99.1. 2080.

Family and domain databases

HAMAP

MF_00526.
[Tree]

InterPro

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

Gene3D

G3DSA:3.40.50.280. B12_bd. 1 hit.

Pfam

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

TIGRFAMs

TIGR01501. MthylAspMutase. 1 hit.

PROSITE

PS51332. B12_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MAMA_CLOTT

Accession

Primary (citable) accession number: Q05488

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)