Reviewed, UniProtKB/Swiss-Prot Q9K3D7 (ARGHA_MORPR)

Names and origin

Protein names

Recommended name:
    Bifunctional protein argHA
Including the following 2 domains:
    1- Recommended name:
            Argininosuccinate lyase
                Short name=Arginosuccinase
                Short name=ASAL
              EC=4.3.2.1
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS
              Short name=NAGS

Gene names

Name:

argHA

Organism

Moritella profunda

Taxonomic identifier

111291 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Moritellaceae › Moritella

Protein attributes

Sequence length	470 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP MF_00006 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_00006
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_00006 Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP MF_00006
Subcellular location	Cytoplasm Probable HAMAP MF_00006.
Miscellaneous	In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (argJ), argA fulfills an anaplerotic role. HAMAP MF_00006
Sequence similarities	In the N-terminal section; belongs to the lyase 1 family. Argininosuccinate lyase subfamily. In the C-terminal section; belongs to the acetyltransferase family. ArgA subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Lyase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP argininosuccinate lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›470	›470	Bifunctional protein argHA HAMAP MF_00006		PRO_0000186814
Regions
	Region	1 – ›470	›470	Argininosuccinate lyase HAMAP MF_00006
Experimental info
	Non-terminal residue	470	1

Sequences

	Sequence		Length	Mass (Da)
	Q9K3D7-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 68046071CE1F761E	FASTA	470	51,907
	10 20 30 40 50 60 MALWGGRFSQ AADARFKNFN DSLRFDYRLA EQDITGSVAW SKALVSVGIL TQDEQLTIEA 70 80 90 100 110 120 ALNDLKLAVL ENPEQILQSD AEDIHSWVET QLIAKVGDLG KKLHTGRSRN DQVATDLKLW 130 140 150 160 170 180 CKQQGEQLLM QLDKTQQQLV SLAREHQHTV LPGYTHLQRA QPVTFSHWCL AYVEMLERDF 190 200 210 220 230 240 SRLTDCLKRL DTCPLGSGAL AGTAYPMDRT ELAHTLGFAS ATLNSLDSVS DRDHVMELMS 250 260 270 280 290 300 TASMSMIHLS RLAEDLIFYN SGESNFIELA DAVTSGSSLM PQKKNPDALE LIRGKTGRVF 310 320 330 340 350 360 GSLSAMLMTL KALPLAYNKD MQEDKEGLFD ALDTWSDCLE MAAMSLVGMK INEERTKEAA 370 380 390 400 410 420 LGGYSNATEL ADYLVAKGVP FRDSHHIVGE AVVAAIAKGV PLEALTLAEF KAFDVLIEDD 430 440 450 460 470 VYHHLSLDET LAKRKAQGGV SPVQVEFALT NAEKRLEERD TSGISIRAAR

References

[1]

"Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase." Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N. J. Bacteriol. 182:1609-1615(2000) [PubMed: 10692366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 2674.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ252020 Genomic DNA. Translation: CAB95018.1.
3D structure databases
SMR	Q9K3D7. Positions 3-456.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.1. 276314. 4.3.2.1. 276314.
Family and domain databases
HAMAP	MF_00006. Arg_succ_lyase. Fused. [Tree] MF_01105. N-acetyl_glu_synth. Fused. Divergent sequence. [Tree]
InterPro	IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. [Graphical view]
PANTHER	PTHR11444:SF3. argH. 1 hit.
Pfam	PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00838. argH. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGHA_MORPR

Accession

Primary (citable) accession number: Q9K3D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
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)