Reviewed, UniProtKB/Swiss-Prot Q8XDS0 (ASPA_ECO57)

Names and origin

Protein names

Recommended name:
    Aspartate ammonia-lyase
      Short name=Aspartase
    EC=4.3.1.1

Gene names

Name:	aspA
Ordered Locus Names:	Z5744, ECs5120

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-aspartate = fumarate + NH3.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.

Ontologies

Keywords
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aspartate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular function	aspartate 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 – 478	478	Aspartate ammonia-lyase		PRO_0000161339
Regions
	Region	143 – 145	3	Substrate binding By similarity
Sites
	Binding site	104	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XDS0-1 [UniParc]. Last modified November 8, 2005. Version 2. Checksum: B6E8432DBF385DEA	FASTA	478	52,356
	10 20 30 40 50 60 MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM 70 80 90 100 110 120 ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE 130 140 150 160 170 180 LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE 190 200 210 220 230 240 FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN 250 260 270 280 290 300 TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL 310 320 330 340 350 360 LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ 370 380 390 400 410 420 LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG 430 440 450 460 470 HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ

References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG59338.1. Different initiation. BA000007 Genomic DNA. Translation: BAB38543.1. Different initiation.
PIR	F86109. H91268.
RefSeq	NP_290772.1. NP_313147.2.
3D structure databases
HSSP	HSSP built from PDB template 1JSW based on UniProtKB P04422.
SMR	Q8XDS0. Positions 1-460.
ModBase	Search...
Genome annotation databases
GeneID	914128. 959984.
GenomeReviews	Gene locus Z5744 in contig AE005174_GR. Gene locus ECs5120 in contig BA000007_GR.
KEGG	ece:Z5744. ecs:ECs5120.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XDS0.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS5120-MON.
Family and domain databases
InterPro	IPR004708. ApsA. IPR003031. D_crystallin. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00839. aspA. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPA_ECO57

Accession

Primary (citable) accession number: Q8XDS0
Secondary accession number(s): Q7A8X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	November 3, 2009
This is version 49 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)