Reviewed, UniProtKB/Swiss-Prot P80077 (GLME_CLOCO)

Names and origin

Protein names

Recommended name:
    Methylaspartate mutase E chain
    EC=5.4.99.1
Alternative name(s):
    Glutamate mutase subunit epsilon

Gene names

Name:

glmE

Organism

Clostridium cochlearium

Taxonomic identifier

1494 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	483 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.
Cofactor	Cobalamin.
Pathway	Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4.
Subunit structure	Heterotetramer of 2 E subunits and 2 S subunits.

Ontologies

Keywords
Ligand	Cobalamin Cobalt
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anaerobic glutamate catabolic process Inferred from electronic annotation. Source: InterPro
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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 483

483

Methylaspartate mutase E chain

PRO_0000087511

Secondary structure

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483

Helix Strand Turn

Details...

Helix

10 – 20

11

Helix

21 – 23

3

Helix

25 – 29

5

Helix

32 – 41

10

Helix

44 – 46

3

Helix

48 – 58

11

Beta strand

62 – 64

3

Helix

72 – 84

13

Beta strand

89 – 94

6

Helix

97 – 100

4

Helix

104 – 117

14

Beta strand

122 – 124

3

Helix

127 – 140

14

Beta strand

146 – 149

4

Helix

156 – 164

9

Beta strand

169 – 171

3

Turn

174 – 181

8

Helix

187 – 206

20

Beta strand

212 – 214

3

Turn

217 – 220

4

Beta strand

221 – 223

3

Helix

226 – 242

17

Beta strand

247 – 253

7

Helix

258 – 278

21

Beta strand

285 – 291

7

Helix

301 – 318

18

Beta strand

321 – 324

4

Turn

328 – 332

5

Helix

337 – 353

17

Turn

354 – 356

3

Helix

363 – 386

24

Turn

387 – 389

3

Helix

391 – 400

10

Beta strand

419 – 422

4

Beta strand

428 – 432

5

Helix

440 – 457

18

Helix

463 – 472

10

Turn

473 – 476

4

Sequences

	Sequence		Length	Mass (Da)
	P80077-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 0789965B945B3F5C	FASTA	483	53,574
	10 20 30 40 50 60 MELKNKKWTD EEFHKQREEV LQQWPTGKEV DLQEAVDYLK KIPAEKNFAE KLVLAKKKGI 70 80 90 100 110 120 TMAQPRAGVA LLDEHIELLR YLQDEGGADF LPSTIDAYTR QNRYDECENG IKESEKAGRS 130 140 150 160 170 180 LLNGFPGVNY GVKGCRKVLE AVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNVP 190 200 210 220 230 240 YAKNVTIEKS LLDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA 250 260 270 280 290 300 AEQGVKNITV GYGECGNMIQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 310 320 330 340 350 360 ESKAFGVIVT ATTIAALAGA TKVIVKTPHE AIGIPTKEAN AAGIKATKMA LNMLEGQRMP 370 380 390 400 410 420 MSKELETEMA VIKAETKCIL DKMFELGKGD LAIGTVKAFE TGVMDIPFGP SKYNAGKMMP 430 440 450 460 470 480 VRDNLGCVRY LEFGNVPFTE EIKNYNRERL QERAKFEGRD VSFQMVIDDI FAVGKGRLIG RPE

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: 7880251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[2]	"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: 1315276] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-26. Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
[3]	"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: 10467146] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). Strain: ATCC 17787 / DSM 1285 / NCIB 10633.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X80997 Genomic DNA. Translation: CAA56923.1.

PIR

I40662.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CB7	X-ray	2.00	B/D	1-483	[»]
1CCW	X-ray	1.60	B/D	1-483	[»]
1I9C	X-ray	1.90	B/D	1-483	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-1101.

BRENDA

5.4.99.1. 2077.

Family and domain databases

InterPro

IPR014348. Cbl-dep_enz_cat-sub.
IPR006396. Glu_mut_E.
IPR014714. Glu_mut_E_C.
[Graphical view]

Gene3D

G3DSA:3.20.20.240. Cobalamin-dep_enz_cat. 1 hit.
G3DSA:3.90.970.10. Glu_mut_E_C. 1 hit.

Pfam

PF06368. Met_asp_mut_E. 1 hit.
[Graphical view]

PIRSF

PIRSF001495. Met_asp_mut_epsi. 1 hit.

TIGRFAMs

TIGR01503. MthylAspMut_E. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GLME_CLOCO

Accession

Primary (citable) accession number: P80077

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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