Reviewed, UniProtKB/Swiss-Prot Q6FMI5 (LYS2_CANGA)

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
Ordered Locus Names:	CAGL0K07788g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	1374 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 By similarity.
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 (fungal 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
Technical term	Complete proteome
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 – 1374	1374	L-aminoadipate-semialdehyde dehydrogenase large subunit		PRO_0000193150
Regions
	Domain	833 – 902	70	Acyl carrier
Amino acid modifications
	Modified residue	865	1	O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6FMI5-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: FF8BF53926B4B184	FASTA	1,374	152,537
	10 20 30 40 50 60 MSWKERLDNP TLSVWPHDYL RPHAEPFVEQ GTYSISIPQL SGDYATLLAA WTALLYRVTG 70 80 90 100 110 120 DDDIVLYVRD NKVLRFTITP ELTFTQLQNK INEQLAELAN VEGTNFDALS ESLQKESGLE 130 140 150 160 170 180 RPPQLFRIAC VTEDLQLDRY THSPLDIGLQ LHESSSDVSI VFNKLLFSQD RITILADQLT 190 200 210 220 230 240 LFLTSVLQNA KQVFTKVSLI TDSSTSILPD PKANLDWCGF VGCIHDIFQD NAEKFPERTC 250 260 270 280 290 300 VVETPPINST KTRTFTYKDI NEASNIVAHY LINTGIKRGD VVMIYSSRGV DLMVCVMGVL 310 320 330 340 350 360 KAGATFSVID PAYPPARQTI YLGVAKPKGL IVIRAAGQLD QLVEDYITKE LDLVSRIPSI 370 380 390 400 410 420 AIQDNGTVEG GSLPSESGDV LASYTELKST RTGVVVGPDS NPTLSFTSGS EGIPKGVLGR 430 440 450 460 470 480 HFSLAYYFSW MAKQFNLSEN DKFTMLSGIA HDPIQRDMFT PLFLGAQLYV PTQDDIGTPG 490 500 510 520 530 540 RLAEWMGKYG CTVTHLTPAM GQLLTAQAVT PFPKLHHAFF VGDILTKRDC LRLQTLAENC 550 560 570 580 590 600 CIVNMYGTTE TQRAVSYFEV TSRSQDPHFL KKLKDVMPAG RGMKNVQLLV VNRNDRTQVC 610 620 630 640 650 660 GVGEIGEIYV RAGGLAEGYR GLPDLNKEKF VNNWFVEEGH WNYLDKDLEA PWKEFWQGPR 670 680 690 700 710 720 DRLYRTGDLG RYLPNGDCEC CGRADDQVKI RGFRIELGEI DTNISQHPLV RENITLVRNN 730 740 750 760 770 780 LEGEKCLVTY MVPRFDKPEL ENFKIEVPSN ISDDPVVCGL IGYSPFTKDL KAFLKKRLAS 790 800 810 820 830 840 YAIPSLIIVL PKLPLNPNGK VDKPKLQFPT VKQLELVAKN SSIDINDSEF NQQEREIRDL 850 860 870 880 890 900 WLECLPTKPT SISPEDSFFD LGGHSILATK MIFTVKKQLN VELPLGTIFK YPTIKAFAAE 910 920 930 940 950 960 VSRLKSTDKI EEETTALTAD YASDAASLID TLPKSYPAAR ALGSPSEMAG PTTVNIFVTG 970 980 990 1000 1010 1020 VTGFLGSFIL SDILNRTVTG VNFKIFAHVR AADETSGLDR IRKAGTVYGT WKEEYANSLQ 1030 1040 1050 1060 1070 1080 VVIGDLSKKN FGLTDDKWSH LSETIDIIIH NGALVHWVYP YSKLRNANVV STINIMNLAS 1090 1100 1110 1120 1130 1140 EGKPKLFNFV SSTSVLDTNH YFELSDKLQQ SGKEGIPESD DLMGSSLGLT SGYGQSKWAA 1150 1160 1170 1180 1190 1200 EHIIRAAGKR GLRGSIIRPG YVTGASYNGS SNTDDFLLRF LKSAVQLGKI PDINNTVNMV 1210 1220 1230 1240 1250 1260 PVDQVARVVV AASINPPCGD DLCVVHVNAH PRIIFKDYLY ELKNYGYDVE IENYEQWKKT 1270 1280 1290 1300 1310 1320 LEEAVIERSE DNALFPLLHM VLGDLEDSTK APELDDKNAI TSLRADIEWT NEDRTKGMGA 1330 1340 1350 1360 1370 TPEQIGIYIS FLESVGFLPH PKHFGDKALP NIKISEQQKE LVASGAGARS SSAA

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380957 Genomic DNA. Translation: CAG61522.1.
RefSeq	XP_448559.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FMI5.
Genome annotation databases
GeneID	2890361.
GenomeReviews	Gene locus CAGL0K07788g in contig CR380957_GR.
KEGG	cgr:CAGL0K07788g.
Phylogenomic databases
HOGENOM	Q6FMI5.
OMA	THLTPAM.
Enzyme and pathway databases
BRENDA	1.2.1.31. 189220.
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. PPantetheine_attach_site. 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_CANGA

Accession

Primary (citable) accession number: Q6FMI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)