Reviewed, UniProtKB/Swiss-Prot Q05514 (MAAL_CLOTT)

Names and origin

Protein names	Recommended name:     Methylaspartate ammonia-lyase     EC=4.3.1.2 Alternative name(s):     Beta-methylaspartase
Organism	Clostridium tetanomorphum
Taxonomic identifier	1553 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	413 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 = mesaconate + NH3.
Cofactor	Cobalamin.
Pathway	Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 2/4.
Subunit structure	Homodimer.

Ontologies

Keywords
Ligand	Cobalamin Cobalt
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylaspartate ammonia-lyase 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 – 413

413

Methylaspartate ammonia-lyase

PRO_0000084547

Secondary structure

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413

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Beta strand

14 – 18

5

Helix

20 – 24

5

Beta strand

28 – 30

3

Beta strand

33 – 36

4

Beta strand

44 – 49

6

Beta strand

52 – 59

8

Beta strand

64 – 69

6

Turn

73 – 76

4

Helix

86 – 96

11

Helix

98 – 101

4

Helix

109 – 118

10

Helix

128 – 146

19

Helix

150 – 158

9

Helix

179 – 186

8

Beta strand

190 – 194

5

Helix

200 – 204

5

Helix

209 – 225

17

Beta strand

234 – 238

5

Helix

242 – 246

5

Turn

247 – 249

3

Helix

251 – 265

15

Beta strand

270 – 273

4

Helix

281 – 298

18

Beta strand

302 – 306

5

Helix

313 – 321

9

Beta strand

325 – 330

6

Helix

333 – 335

3

Helix

339 – 350

12

Beta strand

354 – 357

4

Helix

365 – 378

14

Beta strand

381 – 384

4

Beta strand

387 – 391

5

Helix

392 – 410

19

Sequences

	Sequence		Length	Mass (Da)
	Q05514-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 4451923DB035EF13	FASTA	413	45,534
	10 20 30 40 50 60 MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG ESISVLLVLE 70 80 90 100 110 120 DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK LIGREITNFK PMAEEFDKMT 130 140 150 160 170 180 VNGNRLHTAI RYGITQAILD AVAKTRKVTM AEVIRDEYNP GAEINAVPVF AQSGDDRYDN 190 200 210 220 230 240 VDKMIIKEAD VLPHALINNV EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY 250 260 270 280 290 300 GTIGAAFDVD IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV 310 320 330 340 350 360 DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA NGMGAYCGGT 370 380 390 400 410 CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN EMNRVLALVG RRK

References

[1]	"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], PROTEIN SEQUENCE OF 1-26. Strain: ATCC 15920 / DSM 528 / H1.
[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] OF 1-24, PROTEIN SEQUENCE OF 1-24. Strain: ATCC 15920 / DSM 528 / H1.
[3]	"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] OF 1-71. Strain: NCIMB 11547.
[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 1-15. Strain: NCIMB 11547.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

S48141 Genomic DNA. Translation: AAB24070.1.
X70499 Genomic DNA. Translation: CAA49911.1.
X70695 Genomic DNA. Translation: CAA50027.1.

PIR

B44285.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KCZ	X-ray	1.90	A/B	1-413	[»]
1KD0	X-ray	1.90	A/B	1-413	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-1103.

BRENDA

4.3.1.2. 2080.

Family and domain databases

InterPro

IPR006395. Met_Asp_am_lyase.
[Graphical view]

Pfam

PF07476. MAAL_C. 1 hit.
PF05034. MAAL_N. 1 hit.
[Graphical view]

PIRSF

PIRSF017107. MAL. 1 hit.

TIGRFAMs

TIGR01502. B_methylAsp_ase. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MAAL_CLOTT

Accession

Primary (citable) accession number: Q05514

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 20, 2009
This is version 55 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)