Reviewed, UniProtKB/Swiss-Prot P40976 (LYS2_SCHPO)

Names and origin

Protein names

Recommended name:
    L-aminoadipate-semialdehyde dehydrogenase
    EC=1.2.1.31
Alternative name(s):
    Alpha-aminoadipate reductase
      Short name=Alpha-AR

Gene names

Name:	lys1
ORF Names:	SPAP7G5.04c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH.
Catalytic activity	L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.
Cofactor	Binds 1 phosphopantetheine covalently Potential.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungi route): step 1/3.
Subcellular location	Cytoplasm. Ref.4
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lysine biosynthetic process Ref.3 Inferred from direct assay. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.4 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	L-aminoadipate-semialdehyde dehydrogenase activity Ref.3 Inferred from direct assay. Source: GeneDB_SPombe acyl carrier activity Inferred from electronic annotation. Source: InterPro acyl-CoA binding Ref.3 Inferred from direct assay. Source: GeneDB_SPombe ligase activity Inferred from electronic annotation. Source: InterPro phosphopantetheine binding 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 – 1419	1419	L-aminoadipate-semialdehyde dehydrogenase		PRO_0000193152
Regions
	Domain	885 – 953	69	Acyl carrier
Amino acid modifications
	Modified residue	916	1	O-(pantetheine 4'-phosphoryl)serine Potential
Experimental info
	Mutagenesis	913	1	G → A: No activity. Ref.3
	Mutagenesis	916	1	S → A or T: No activity. Ref.3
	Sequence conflict	90 – 91	2	MT → IA in AAC15909. Ref.1
	Sequence conflict	196	1	Missing in AAC15909. Ref.1
	Sequence conflict	487	1	D → DG in AAC15909. Ref.1
	Sequence conflict	500	1	R → G in AAC15909. Ref.1
	Sequence conflict	600 – 602	3	Missing Ref.1
	Sequence conflict	620 – 621	2	AR → GP in AAC15909. Ref.1
	Sequence conflict	712	1	Y → S in AAC15909. Ref.1
	Sequence conflict	926 – 928	3	LRK → PSQ in AAC15909. Ref.1
	Sequence conflict	1203 – 1205	3	VVV → AAA in AAC15909. Ref.1
	Sequence conflict	1225 – 1228	4	LVRM → WSK in AAC15909. Ref.1
	Sequence conflict	1239	1	P → A in AAC15909. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40976-1 [UniParc]. Last modified February 21, 2001. Version 3. Checksum: 09AFBEFE09F21A0C	FASTA	1,419	156,894
	10 20 30 40 50 60 MSQTAPSDTE YNQRLERWSE RLKSQTISHL PTDYSRPVPS RLVEAVFERT LPEDAKTALI 70 80 90 100 110 120 KVYVAAQAKG ILVTPFNILL TIFIILVSRM TGDEDISIGT SSENAIPFVL RTFIQPSDSF 130 140 150 160 170 180 LDLLAKVCDL EKEGSSDAVD FSDLINFLNA KLSKKDDPRK TLVHLRFYNA PDAPSENFLS 190 200 210 220 230 240 TTGLDVDLTV LVSVKKPSDQ LTSLRSQFTF PDLQLKLIYN QLLFSESRVN IVADQLLKLV 250 260 270 280 290 300 VSASKDVTGP IGALDLMTPT QMNVLPDPTV DLDWSGYRGA IQDIFASNAA KFPDRECIVV 310 320 330 340 350 360 TPSVTIDAPV TSYTYRQIDE SSNILAHHLV KNGIERGDVV MVYAYRGVDL VVAVMGVLKA 370 380 390 400 410 420 GATFSVIDPA YPPARQIIYL SVAKPRALVV LEDAGVLSPT VVEYVEKSLE LKTYVPALKL 430 440 450 460 470 480 AKDGSLTGGS VSKGADDILQ HVLHLKSEQT GVVVGPDSTP TLSFTSGSEG IPKGVKGRHF 490 500 510 520 530 540 SLAYYFDWMA QEFNLSESDR FTMLSGIAHD PIQRDIFTPL FLGASLIVPT AEDIGTPGQL 550 560 570 580 590 600 AQWANKYKVT VTHLTPAMGQ LLAAQADEPI PSLHHAFFVG DILTKRDCLR LQVLANNVNV 610 620 630 640 650 660 VNMYGTTETQ RSVSYFVVPA RSQDQTFLES QKDVIPAGRG MKNVQLLVIN RFDTNKICGI 670 680 690 700 710 720 GEVGEIYLRA GGLAEGYLGN DELTSKKFLK SWFADPSKFV DRTPENAPWK PYWFGIRDRM 730 740 750 760 770 780 YRSGDLGRYL PTGNVECSGR ADDQIKIRGF RIELGEINTH LSRHPNVREN ITLVRRDKDE 790 800 810 820 830 840 EPTLVAYIVP QGLNKDDFDS ATESEDIVVN GLKKYRKLIH DIREYLKTKL PSYAIPSVIV 850 860 870 880 890 900 PLHKMPLNPN GKIDKPALPF PDTSQLAAAS RSHSKHGVDE TLTATERDIR DIWLRIIPHA 910 920 930 940 950 960 TDVNKKASFF DIGGHSILAT RLIFELRKKF AVNVPLGLVF SEPTIEGLAK EIERMKSGEM 970 980 990 1000 1010 1020 ISVMDIGKEE TREPEIEYGK DALDLVDLIP KEFPTSKDLG IDEPKTVFLT GANGYLGVFI 1030 1040 1050 1060 1070 1080 LRDLMTRSSN LKVIALVRAS SEEHGLKRLK DSCTAYGVWD ESWAQKISVV NGDLALENWG 1090 1100 1110 1120 1130 1140 IEERKWNKLT EVVDYVIHNG ALVHWVYPYS KLRGPNVMGT ITALKLCSLG KGKSLSFVSS 1150 1160 1170 1180 1190 1200 TSTVDTEYYV NLSNEITSKG GNGIPESDPL QGSSKDLHTG YGQSKWVSEY LVRQAGLRGL 1210 1220 1230 1240 1250 1260 RGVVVRPGYI LGDSKSGAIN TDDFLVRMVK GCIELGLYPN INNTVNMVPA DHVARVVTAS 1270 1280 1290 1300 1310 1320 AFHPEQGVIV AHVTSHPRLR FNQFLGTLST FGFNTKLSEY VNWRIALERF VINESHDSAL 1330 1340 1350 1360 1370 1380 YPLLHFVLDN LPANTKAPEL DDTNTREILK RDASWTNVDV SNGAAILEHE MGLYLSYLVA 1390 1400 1410 IGFLPKPTLE GKKLPEVKIN EATLEKLASA GGRGGAPTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular properties of the lys1+ gene and the regulation of alpha-aminoadipate reductase in Schizosaccharomyces pombe." Ford R.A., Bhattacharjee J.K. Curr. Genet. 28:131-137(1995) [PubMed: 8590464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe." Guo S., Bhattacharjee J.K. Yeast 21:1279-1288(2004) [PubMed: 15546125] [Abstract] Cited for: MUTAGENESIS OF GLY-913 AND SER-916. Strain: ATCC 38366 / 972.
[4]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U15923 Genomic DNA. Translation: AAC15909.1. CU329670 Genomic DNA. Translation: CAB88271.1.
PIR	S57264.
RefSeq	NP_594314.1.
3D structure databases
HSSP	HSSP built from PDB template 1AMU based on UniProtKB P14687.
ModBase	Search...
Genome annotation databases
GeneID	2542079.
KEGG	spo:SPAP7G5.04c.
NMPDR	fig|4896.1.peg.4284.
Organism-specific databases
GeneDB_Spombe	SPAP7G5.04c.
Phylogenomic databases
OMA	P40976. THLTPAM.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001916-MON.
BRENDA	1.2.1.31. 653.
Gene expression databases
ArrayExpress	P40976.
Family and domain databases
InterPro	IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. IPR000873. AMP-dep_Synth/Lig. IPR014397. L-NH2adipate-semiAld_DH_lsu. IPR013120. Male_sterile_NAD-bd. IPR016040. NAD(P)-bd_dom. IPR006163. Phsphopanteth_bd. IPR006162. Ppantne_S. IPR010080. Thioester_reductase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00501. AMP-binding. 1 hit. PF07993. NAD_binding_4. 1 hit. PF00550. PP-binding. 1 hit. [Graphical view]
PIRSF	PIRSF001617. Alpha-AR. 1 hit.
TIGRFAMs	TIGR01733. AA-adenyl-dom. 1 hit. TIGR03443. alpha_am_amid. 1 hit. TIGR01746. Thioester-redct. 1 hit.
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00455. AMP_BINDING. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS2_SCHPO

Accession

Primary (citable) accession number: P40976
Secondary accession number(s): Q9P770

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 21, 2001
Last modified:	June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)