Q980X1 (ARGC_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase
Short name=AGPR
EC=1.2.1.-
EC=1.2.1.38

Alternative name(s):
N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase
Short name=NAGSA dehydrogenase

Gene names

Name:	argC
Synonyms:	lysY
Ordered Locus Names:	SSO0155

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways. HAMAP MF_00150
Catalytic activity	N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP MF_00150 N(2)-acetyl-L-aminoadipate-semialdehyde + NADP+ + phosphate = N(2)-acetyl-L-gamma-aminoadipyl phosphate + NADPH. HAMAP MF_00150
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP MF_00150 Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. HAMAP MF_00150
Subcellular location	Cytoplasm Probable HAMAP MF_00150.
Sequence similarities	Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase HAMAP MF_00150		PRO_0000112498
Sites
	Active site	153	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q980X1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: CAA3053D6E08A188	FASTA	352	38,685
	10 20 30 40 50 60 MKDKVRVAVV GGSGYTGGEL LRILVTHPKT EISVITSREY AGKPVSLIHP NLRGLISLNF 70 80 90 100 110 120 TNFSIDKISD KADAIFLALP HGVSLNYAPK LLDLGLTVVD LSADFRLKNP ELYKIWYNYE 130 140 150 160 170 180 HPYPDLLDKA VYGLPELHYE ELKNAKLIAS PGCNATATIL ALAPIVATKI TDEKKFISDV 190 200 210 220 230 240 KVGSSEGGAK PSEGSHHPER QNAIRPYEAE GHRHAAEAEQ ELSRIAKANI SVSIVPHAVS 250 260 270 280 290 300 SIRGALASAH TWLTNELEEI EIWKKIAEFY RGKRFIRIIR GNIHPYPDPK FVIGSNFADI 310 320 330 340 350 GFAVEKRISR LTTFSAIDNL MKGAAGQAVQ AFNISMGFNE DDGLKLVPLR PA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]	"The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability." Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W.M., van der Oost J. J. Biol. Chem. 277:29537-29549(2002) [PubMed: 12042311] [Abstract] Cited for: INVOLVEMENT IN LYSINE BIOSYNTHESIS. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006641 Genomic DNA. Translation: AAK40501.1. BK000545 Genomic DNA. Translation: DAA00049.1.
PIR	F90155.
RefSeq	NP_341711.1. NC_002754.1.
3D structure databases
ProteinModelPortal	Q980X1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1453328.
GenomeReviews	Gene locus SSO0155 in contig AE006641_GR.
KEGG	sso:SSO0155.
NMPDR	fig|273057.1.peg.134.
Phylogenomic databases
HOGENOM	HBG294213.
OMA	VYRYPEP.
ProtClustDB	PRK00436.
Enzyme and pathway databases
BioCyc	SSOL273057:SSO0155-MONOMER.
Family and domain databases
HAMAP	MF_00150. ArgC_type1. [Tree]
InterPro	IPR023013. AGPR_AS. IPR000706. AGPR_type-1. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00145.
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01850. ArgC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGC_SULSO

Accession

Primary (citable) accession number: Q980X1
Secondary accession number(s): Q7SI96

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 1, 2001
Last modified:	December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program