Q05509 (GLME_CLOTT) Reviewed, UniProtKB/Swiss-Prot

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:

mutE

Organism

Clostridium tetanomorphum

Taxonomic identifier

1553 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
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	Possible heterotetramer, composed of two E chains and two S chains. E exists as a homodimer and S as a monomer.

Ontologies

Keywords
Ligand	Cobalamin Cobalt
Molecular function	Isomerase
Technical term	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 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 – 485	485	Methylaspartate mutase E chain		PRO_0000087512
Experimental info
	Sequence conflict	8	1	W → L AA sequence Ref.4
	Sequence conflict	12	1	E → G AA sequence Ref.4
	Sequence conflict	17	1	R → A AA sequence Ref.4
	Sequence conflict	19	1	E → G AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q05509 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 131792A392CACCC0	FASTA	485	53,741
	10 20 30 40 50 60 MELKNKKWTD EEFFKQREEV LKQWPTGKEV DLQEAVDYLK KVPTEKNFAD KLVRAKEAGI 70 80 90 100 110 120 TLAQPRAGVA LLDEHINLLR YLQDEGGADL LPSTIDAYTR QNRYEECEIG IKESEKAGRS 130 140 150 160 170 180 LLNGFPGVNH GVKGCRKVLE SVNLPLQARH GTPDSRLLAE IIHAGGWTSN EGGGISYNIP 190 200 210 220 230 240 YAKSVPIDKC LKDWQYCDRL VGFYEEQGVH INREPFGPLT GTLVPPSMSN AVGITEALLA 250 260 270 280 290 300 AEQGVKNITV GYGECGNMLQ DIAALRCLEE QTNEYLKAYG YNDVFVTTVF HQWMGGFPQD 310 320 330 340 350 360 ESKAFGVIVT ATTIASLAGA TKVIVKTPHE AIGIPTKEAN ASGIKATKMA LNMLEGQRMP 370 380 390 400 410 420 MSKELETEMA IIKAETKCIL DKMFELGKGD LAVGTVKAFE TGVMDIPFGP SKYNAGKMMP 430 440 450 460 470 480 VRDNLGCVRY LEFGNVPFTE ELKNYNRERL AERAKFEGRE VSFQMVIDDI FAVGKGRLIG RPENK

References

[1]	"Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes." Holloway D.E., Marsh E.N.G. FEBS Lett. 317:44-48(1993) [PubMed: 8428631] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 15920 / DSM 528 / H1.
[3]	"Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein." Goda S.K., Minton N.P., Botting N.P., Gani D. Biochemistry 31:10747-10756(1992) [PubMed: 1420191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-485. Strain: ATCC 15920 / DSM 528 / H1.
[4]	"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: PROTEIN SEQUENCE OF 1-20. Strain: NCIMB 11547.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70499 Genomic DNA. Translation: CAA49910.1. X70695 Genomic DNA. Translation: CAA50026.1. S48141 Genomic DNA. Translation: AAB24069.1.
PIR	S32433.
3D structure databases
ProteinModelPortal	Q05509.
SMR	Q05509. Positions 1-483.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR016176. Cbl-dep_enz_cat. 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.
SUPFAM	SSF51703. Cbl-dep_enz_cat. 1 hit.
TIGRFAMs	TIGR01503. MthylAspMut_E. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLME_CLOTT

Accession

Primary (citable) accession number: Q05509

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 31, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program