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Protein

L-2-aminoadipate reductase large subunit

Gene

LYS2

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.By similarity

Catalytic activityi

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.By similarity
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + ATP.By similarity

Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

Pathwayi: L-lysine biosynthesis via AAA pathway

This protein is involved in step 1 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. L-2-aminoadipate reductase large subunit (LYS2)
  2. no protein annotated in this organism
  3. Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (LYS1)
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Lysine biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00033; UER00032

Names & Taxonomyi

Protein namesi
Recommended name:
L-2-aminoadipate reductase large subunit (EC:1.2.1.31By similarity, EC:1.2.1.95By similarity)
Alternative name(s):
Alpha-aminoadipate reductase
Short name:
Alpha-AR
L-aminoadipate-semialdehyde dehydrogenase
Gene namesi
Name:LYS2
Ordered Locus Names:CAGL0K07788g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome K

Organism-specific databases

CGDiCAL0133971 CAGL0K07788g
EuPathDBiFungiDB:CAGL0K07788g

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931501 – 1374L-2-aminoadipate reductase large subunitAdd BLAST1374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei865O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiQ6FMI5

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

STRINGi284593.XP_448559.1

Structurei

3D structure databases

ProteinModelPortaliQ6FMI5
SMRiQ6FMI5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini828 – 905CarrierPROSITE-ProRule annotationAdd BLAST78

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1178 Eukaryota
COG1020 LUCA
COG3320 LUCA
HOGENOMiHOG000191209
InParanoidiQ6FMI5
KOiK00143
OMAiMIYAYRG
OrthoDBiEOG092C07V5

Family and domain databases

CDDicd05235 SDR_e1, 1 hit
Gene3Di1.10.1200.10, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR014397 Lys2
IPR013120 Male_sterile_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR010080 Thioester_reductase-like_dom
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PF07993 NAD_binding_4, 1 hit
PF00550 PP-binding, 1 hit
SMARTiView protein in SMART
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
TIGR03443 alpha_am_amid, 1 hit
TIGR01746 Thioester-redct, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 1 hit

Sequencei

Sequence statusi: Complete.

Q6FMI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWKERLDNP TLSVWPHDYL RPHAEPFVEQ GTYSISIPQL SGDYATLLAA
60 70 80 90 100
WTALLYRVTG DDDIVLYVRD NKVLRFTITP ELTFTQLQNK INEQLAELAN
110 120 130 140 150
VEGTNFDALS ESLQKESGLE RPPQLFRIAC VTEDLQLDRY THSPLDIGLQ
160 170 180 190 200
LHESSSDVSI VFNKLLFSQD RITILADQLT LFLTSVLQNA KQVFTKVSLI
210 220 230 240 250
TDSSTSILPD PKANLDWCGF VGCIHDIFQD NAEKFPERTC VVETPPINST
260 270 280 290 300
KTRTFTYKDI NEASNIVAHY LINTGIKRGD VVMIYSSRGV DLMVCVMGVL
310 320 330 340 350
KAGATFSVID PAYPPARQTI YLGVAKPKGL IVIRAAGQLD QLVEDYITKE
360 370 380 390 400
LDLVSRIPSI AIQDNGTVEG GSLPSESGDV LASYTELKST RTGVVVGPDS
410 420 430 440 450
NPTLSFTSGS EGIPKGVLGR HFSLAYYFSW MAKQFNLSEN DKFTMLSGIA
460 470 480 490 500
HDPIQRDMFT PLFLGAQLYV PTQDDIGTPG RLAEWMGKYG CTVTHLTPAM
510 520 530 540 550
GQLLTAQAVT PFPKLHHAFF VGDILTKRDC LRLQTLAENC CIVNMYGTTE
560 570 580 590 600
TQRAVSYFEV TSRSQDPHFL KKLKDVMPAG RGMKNVQLLV VNRNDRTQVC
610 620 630 640 650
GVGEIGEIYV RAGGLAEGYR GLPDLNKEKF VNNWFVEEGH WNYLDKDLEA
660 670 680 690 700
PWKEFWQGPR DRLYRTGDLG RYLPNGDCEC CGRADDQVKI RGFRIELGEI
710 720 730 740 750
DTNISQHPLV RENITLVRNN LEGEKCLVTY MVPRFDKPEL ENFKIEVPSN
760 770 780 790 800
ISDDPVVCGL IGYSPFTKDL KAFLKKRLAS YAIPSLIIVL PKLPLNPNGK
810 820 830 840 850
VDKPKLQFPT VKQLELVAKN SSIDINDSEF NQQEREIRDL WLECLPTKPT
860 870 880 890 900
SISPEDSFFD LGGHSILATK MIFTVKKQLN VELPLGTIFK YPTIKAFAAE
910 920 930 940 950
VSRLKSTDKI EEETTALTAD YASDAASLID TLPKSYPAAR ALGSPSEMAG
960 970 980 990 1000
PTTVNIFVTG VTGFLGSFIL SDILNRTVTG VNFKIFAHVR AADETSGLDR
1010 1020 1030 1040 1050
IRKAGTVYGT WKEEYANSLQ VVIGDLSKKN FGLTDDKWSH LSETIDIIIH
1060 1070 1080 1090 1100
NGALVHWVYP YSKLRNANVV STINIMNLAS EGKPKLFNFV SSTSVLDTNH
1110 1120 1130 1140 1150
YFELSDKLQQ SGKEGIPESD DLMGSSLGLT SGYGQSKWAA EHIIRAAGKR
1160 1170 1180 1190 1200
GLRGSIIRPG YVTGASYNGS SNTDDFLLRF LKSAVQLGKI PDINNTVNMV
1210 1220 1230 1240 1250
PVDQVARVVV AASINPPCGD DLCVVHVNAH PRIIFKDYLY ELKNYGYDVE
1260 1270 1280 1290 1300
IENYEQWKKT LEEAVIERSE DNALFPLLHM VLGDLEDSTK APELDDKNAI
1310 1320 1330 1340 1350
TSLRADIEWT NEDRTKGMGA TPEQIGIYIS FLESVGFLPH PKHFGDKALP
1360 1370
NIKISEQQKE LVASGAGARS SSAA
Length:1,374
Mass (Da):152,537
Last modified:July 19, 2004 - v1
Checksum:iFF8BF53926B4B184
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380957 Genomic DNA Translation: CAG61522.1
RefSeqiXP_448559.1, XM_448559.1

Genome annotation databases

EnsemblFungiiCAG61522; CAG61522; CAGL0K07788g
GeneIDi2890361
KEGGicgr:CAGL0K07788g

Similar proteinsi

Entry informationi

Entry nameiLYS2_CANGA
AccessioniPrimary (citable) accession number: Q6FMI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 19, 2004
Last modified: May 23, 2018
This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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