Reviewed, UniProtKB/Swiss-Prot Q59200 (ASPA_CORGL)

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:	Cgl1503, cg1697

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	526 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.
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 – 526	526	Aspartate ammonia-lyase		PRO_0000161337
Regions
	Region	194 – 196	3	Substrate binding By similarity
Sites
	Binding site	155	1	Substrate By similarity
Experimental info
	Sequence conflict	138	1	E → G in BAA04987. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q59200-1 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 6C792698A8EA9093	FASTA	526	57,569
	10 20 30 40 50 60 MSKTSNKSSA DSKNDAKAED IVNGENQIAT NESQSSDSAA VSERVVEPKT TVQKKFRIES 70 80 90 100 110 120 DLLGELQIPS HAYYGVHTLR AVDNFQISRT TINHVPDFIR GMVQVKKAAA LANRRLHTLP 130 140 150 160 170 180 AQKAEAIVWA CDQILIEERC MDQFPIDVFQ GGAGTSLNMN TNEVVANLAL EFLGHEKGEY 190 200 210 220 230 240 HILHPMDDVN MSQSTNDSYP TGFRLGIYAG LQTLIAEIDE LQVAFRHKGN EFVDIIKMGR 250 260 270 280 290 300 TQLQDAVPMS LGEEFRAFAH NLAEEQTVLR EAANRLLEVN LGATAIGTGV NTPAGYRHQV 310 320 330 340 350 360 VAALSEVTGL ELKSARDLIE ATSDTGAYVH AHSAIKRAAM KLSKICNDLR LLSSGPRAGL 370 380 390 400 410 420 NEINLPPRQA GSSIMPAKVN PVIPEVVNQV CFKVFGNDLT VTMAAEAGQL QLNVMEPVIG 430 440 450 460 470 480 ESLFQSLRIL GNAAKTLREK CVVGITANAD VCRAYVDNSI GIITYLNPFL GHDIGDQIGK 490 500 510 520 EAAETGRPVR ELILEKKLMD EKTLEAVLSK ENLMHPMFRG RLYLEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence determination of the aspartase-encoding gene from Brevibacterium flavum MJ233." Asai Y., Inui M., Vertes A., Kobayashi M., Yukawa H. Gene 158:87-90(1995) [PubMed: 7789816] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MJ233.
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D25316 Genomic DNA. Translation: BAA04987.1. BA000036 Genomic DNA. Translation: BAB98896.1. BX927152 Genomic DNA. Translation: CAF21511.1.
PIR	JC4101.
RefSeq	NP_600719.1. YP_225787.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSW based on UniProtKB P04422.
ModBase	Search...
Genome annotation databases
GeneID	1019476. 3343809.
GenomeReviews	Gene locus Cgl1503 in contig BA000036_GR. Gene locus cg1697 in contig BX927147_GR.
KEGG	cgb:cg1697. cgl:NCgl1446.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q59200.
OMA	GKICAQT.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG1697-MON.
BRENDA	4.3.1.1. 812.
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_CORGL

Accession

Primary (citable) accession number: Q59200

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2002
Last modified:	November 3, 2009
This is version 57 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)