Reviewed, UniProtKB/Swiss-Prot Q12572 (LYS2_CANAL)

Names and origin

Protein names

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

Gene names

Name:

LYS2

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Subunit structure	Heterodimer of an alpha and a beta subunit By similarity.
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
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-aminoadipate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro 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 – 1391	1391	L-aminoadipate-semialdehyde dehydrogenase large subunit		PRO_0000193149
Regions
	Domain	852 – 902	51	Acyl carrier
Amino acid modifications
	Modified residue	884	1	O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q12572-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: B7E641866235BCDD	FASTA	1,391	154,741
	10 20 30 40 50 60 MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA VFAALVYRLT 70 80 90 100 110 120 GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE YENNISQINY KALSEVSHRI 130 140 150 160 170 180 KEAKGLDENP GLFRLSYQHA HSNQQLNTTV EGSIRDLAIY TDGTKFTIYY NALLYSHERV 190 200 210 220 230 240 VICGEQFAQL TTVSGDTDTV IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN 250 260 270 280 290 300 KHPDRTCVVE TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD 310 320 330 340 350 360 LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ LVVDYISNEL 370 380 390 400 410 420 DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP AGVIVGPDSR PTLSFTSGSE 430 440 450 460 470 480 GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD KFTILSGIAH DPIQRDMFTP LFLGAQLLVP 490 500 510 520 530 540 TADDIGTPGK LADWMAKYGA TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR 550 560 570 580 590 600 LQSLAENVFI VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV 610 620 630 640 650 660 NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW IEQDEANKKS 670 680 690 700 710 720 SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ VKIRGFRIEL GEIDTHLSQH 730 740 750 760 770 780 PLVRENVTLV RRDKNEEPTL ISYIVPKDSP ELKTFFADVD FPLKKSNDPI VKGLVAYREL 790 800 810 820 830 840 IKDIKGYLKK KLASYAIPTI IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD 850 860 870 880 890 900 AQAAEEENLT KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE 910 920 930 940 950 960 IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK ELSKSALLES 970 980 990 1000 1010 1020 YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD IKVYAHVRAS SKEAGLQRLR 1030 1040 1050 1060 1070 1080 QTGITYGIWD ENWAEKIEIV LGDLSKEKFG LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ 1090 1100 1110 1120 1130 1140 LRMLNVIGTI NVFNMAGEVK LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ 1150 1160 1170 1180 1190 1200 GSAKGLGNGY GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG 1210 1220 1230 1240 1250 1260 SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI LFNNFLGCLK 1270 1280 1290 1300 1310 1320 AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD NLPQDTKAPE LDDSNAAKSL 1330 1340 1350 1360 1370 1380 KQDSKYTGED FSAGKGVDLD QTGVYISYLI KIGFLPKPTG TGEKKLPEVE ISDESLKLIS 1390 GGAGARGSAA K

References

[1]

"Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the alpha-aminoadipate reductase." Suvarna K., Seah L., Bhattacherjee V., Bhattacharjee J.K. Curr. Genet. 33:268-275(1998) [PubMed: 9560434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 11651 / B792 / 171D.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U58133 Genomic DNA. Translation: AAC02241.1.
3D structure databases
HSSP	HSSP built from PDB template 1AMU based on UniProtKB P14687.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.31. 1124.
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. IPR006163. Phsphopanteth_bd. IPR006162. Ppantne_S. IPR010080. Thioester_reductase. [Graphical view]
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS2_CANAL

Accession

Primary (citable) accession number: Q12572

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1999
Last modified:	June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)