Q9K3D6 (ARGHA_MORAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional protein ArgHA

Including the following 2 domains:

1. Argininosuccinate lyase
   Short name=ASAL
   Short name=Arginosuccinase
   EC=4.3.2.1
2. 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 abyssi

Taxonomic identifier

111292 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Moritellaceae › Moritella

Protein attributes

Sequence length	629 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP-Rule MF_00006 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP-Rule MF_00006
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP-Rule MF_00006 Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP-Rule MF_00006
Subcellular location	Cytoplasm By similarity.
Miscellaneous	In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role. HAMAP-Rule 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. Contains 1 N-acetyltransferase domain.

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: EC argininosuccinate 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 – 629	629	Bifunctional protein ArgHA HAMAP-Rule MF_00006		PRO_0000186813
Regions
	Domain	464 – 598	135	N-acetyltransferase
	Region	1 – 499	499	Argininosuccinate lyase HAMAP-Rule MF_00006
	Region	500 – 629	130	Amino-acid acetyltransferase HAMAP-Rule MF_00006

Sequences

	Sequence		Length	Mass (Da)
	Q9K3D6 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A9EF306A299539BF	FASTA	629	69,497
	10 20 30 40 50 60 MALWGGRFSQ AADARFKSFN DSLRFDYRLA EQDITGSVAW SKALVSVGIL TQDEQLTIEA 70 80 90 100 110 120 ALNDLKLAVL ENPEQILQSD AEDIHSWVET QLIAKVGDLG KKLHTGRSRN DQVATDLKLW 130 140 150 160 170 180 CKQQGQQLLM QLDKTQQQLV SLAREHQHTV LPGYTHLQRA QPVTFSHWCL AYVEMLERDF 190 200 210 220 230 240 SRLTDCLKRL DTCPLGSGAL AGTAYPMDRT ELAHSLGFGS ATLNSLDSVS DRDHVMELMC 250 260 270 280 290 300 TASMSMIHLS RLAEDLIFYN SGESNFIELA DAVTSGSSLM PQKKNPDALE LIRGKTGRVF 310 320 330 340 350 360 GSLSAMLMTL KALPLAYNKD MQEDKEGLFD ALDTWSDCLE MAAMSLVGMK INEARTKEAA 370 380 390 400 410 420 LGGYSNATEL ADYLVAKGVP FRDSHHIVGE AVVAAIAKGV PLEALTLAEF KAFDVLIEDD 430 440 450 460 470 480 VYHHLSLDET LAKRKALGGV SPVQVEFALT NAEKRLEERD TSGISIRAAR LTDLDDIERM 490 500 510 520 530 540 VNYWANIGEN LPRSRSDLVK AVGTFAVTEK HNQVTGCASI YVYDTGLAEL RSLGIEPGYQ 550 560 570 580 590 600 GGGQGKAVVE YMLRKAEQMA IQKVFVLTRV PEFFMKLGFR STSKSMLPEK VLKDCDMCPR 610 620 QHACDEVALE FKLNVVGQTI NLKAEKLAS

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 2693.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ252021 Genomic DNA. Translation: CAB95024.1.
3D structure databases
ProteinModelPortal	Q9K3D6.
SMR	Q9K3D6. Positions 3-456.
ModBase	Search...
Proteomic databases
PRIDE	Q9K3D6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00068; UER00106. UPA00068; UER00114.
Family and domain databases
Gene3D	1.10.275.10. 1 hit. 3.40.630.30. 1 hit.
HAMAP	MF_00006. Arg_succ_lyase. Fused. MF_01105. N-acetyl_glu_synth. Fused. Divergent sequence.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR009049. Argininosuccinate_lyase. IPR011244. ASAL_AGS_AcTrfase. IPR003031. D_crystallin. IPR024083. Fumarase/histidase_N. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR000182. GNAT_dom. IPR008948. L-Aspartase-like. [Graphical view]
PANTHER	PTHR11444:SF3. PTHR11444:SF3. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PIRSF	PIRSF036456. ASAL_AGS. 1 hit.
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00838. argH. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGHA_MORAB

Accession

Primary (citable) accession number: Q9K3D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program