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UniProtKB - O74298 (LYS2_PENCH)
Protein
L-2-aminoadipate reductase large subunit
Gene
lys2
Organism
Penicillium chrysogenum (Penicillium notatum)
Status
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 similarityCatalytic activityi
- EC:1.2.1.31By similarity
- EC:1.2.1.31By similarity
- (S)-2-amino-6-oxohexanoate + AMP + diphosphate + NADP+ = ATP + H+ + L-2-aminoadipate + NADPHBy similarityEC:1.2.1.95By similarity
Cofactori
pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity
: L-lysine biosynthesis via AAA pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route). 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
- L-aminoadipate-semialdehyde dehydrogenase activity Source: UniProtKB-EC
- phosphopantetheine binding Source: InterPro
GO - Biological processi
- lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Amino-acid biosynthesis, Lysine biosynthesis |
Ligand | NADP |
Enzyme and pathway databases
UniPathwayi | UPA00033;UER00032 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:lys2 |
Organismi | Penicillium chrysogenum (Penicillium notatum) |
Taxonomic identifieri | 5076 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Penicillium › Penicillium chrysogenum species complex |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000193151 | 1 – 1409 | L-2-aminoadipate reductase large subunitAdd BLAST | 1409 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 896 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinProteomic databases
PRIDEi | O74298 |
Interactioni
Subunit structurei
Heterodimer of an alpha and a beta subunit.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 858 – 937 | CarrierPROSITE-ProRule annotationAdd BLAST | 80 |
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family.Curated
Family and domain databases
CDDi | cd05235, SDR_e1, 1 hit |
Gene3Di | 1.10.1200.10, 1 hit 3.30.300.30, 1 hit 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR001242, Condensatn IPR013120, Far_NAD-bd IPR014397, Lys2 IPR036291, NAD(P)-bd_dom_sf IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR010080, Thioester_reductase-like_dom |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF00668, Condensation, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 1 hit |
SMARTi | View protein in SMART SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit TIGR03443, alpha_am_amid, 1 hit TIGR01746, Thioester-redct, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 1 hit |
i Sequence
Sequence statusi: Complete.
O74298-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAVGTASLQD RLETWAQRLK NLTVSPLTRD YPDTQKTDSK RVIEAFESLQ
60 70 80 90 100
LPKAKLTGSS SSFIAFLTAF IILVARLTGD EDIAVGTNSN EDGRAFVIRV
110 120 130 140 150
PIDTSESFAQ LYAKVDKAYK EGSSQIVPLG SLRSYIQEKS KSERTPVLFR
160 170 180 190 200
FAAYDAPASS QDYPANTFDT TDLVVNVAPG SAEVELGAYY NQRLFSSARI
210 220 230 240 250
AFILKQLASI ASNAAANPDE AIGRIDLMTE DQRALLPDPT CNLNWSNFRG
260 270 280 290 300
AIHDIFTANA ERHPEKLCVV ETQSSSSPHR EFTYRQINEA SNILGHHLVR
310 320 330 340 350
SGIQRGEVVM VYAYRGVDLV VAVMGILKAG ATFSVIDPAY PPERQNIYLD
360 370 380 390 400
VARPRALVNI AKATKDAGEL SDIVRTFIDE NLELRTEIPA LALLDDGTLA
410 420 430 440 450
GGSINGQDVF ANDVALKSKP TGVVVGPDSI PTLSFTSGSE GRPKGVRGRH
460 470 480 490 500
FSLAYYFPWM SETFKLTPDE KFTMLSGIAH DPIQRDIFTP LFLGAQLLVP
510 520 530 540 550
AREDIQNEKL AEWIEKYGAT ITHLTPAMGQ ILVGGASAQF PALHHAFFVG
560 570 580 590 600
DILIKRDCRS LQGLAPNVSI VNMYGTTETQ RAVSYYEIPS YASNEGYLNN
610 620 630 640 650
MKDVIMAGRG MLDVQMLVVN RYDPTRLCAI GEVGEIYVRA GGLAEGYLGS
660 670 680 690 700
PELSAKKFLN NWFVNPEIWA EKDQAESRNE PWRQFYVGPR DRLYRSGDLG
710 720 730 740 750
RYTPSGDVEC SGRADDQVKI RGFRIELGEI DTHLSQHPLV RENVTLVRRD
760 770 780 790 800
KDEEPTLVSY FVPDMNKWAS WLESKGLKDD DSDSEGMVGL LRRFRPLRDD
810 820 830 840 850
AREHLRTKLP TYAVPTVIIP LKRMPLNPNG KIDKPALPFP DTAELSAAAP
860 870 880 890 900
RRASSALQAL SETEQTLAQV WAKLIPNVTS RMIGPDDSFF DLGGHSILAQ
910 920 930 940 950
QMFFELRRKW RVIDISMNAI FRSPTLKGFA SEIDRLLAME SFATSDDKTL
960 970 980 990 1000
AVQAANEPDD EYSKDAVQLV NELPKTFPQR TEAMLTSEPT VFLTGATGFL
1010 1020 1030 1040 1050
GAHILRDLLT RKSPSTKVVA LVRAKTEELA LERLRSTCRA YGFWDEAWTA
1060 1070 1080 1090 1100
KLQAVCGDLG KPQFGLSQSV WDDLTNRVDA VIHNGALVHW VYPYATLRPA
1110 1120 1130 1140 1150
NVMGTIDALK LCASGKAKQF AFVSSTSALD KDRYVQESER IIAAGGNGIS
1160 1170 1180 1190 1200
EDDDMEGSRV GLGTGYGQSK WAGEYLVKEA GRRGLRGTIV RSGYVLGDSV
1210 1220 1230 1240 1250
TGTTNTDDFL IRMLKGCIQI GLRPNIFNTV NMVPVDHVAR IVIATAFHPP
1260 1270 1280 1290 1300
ATGVNVAHVT GHPRLRFNQF LGALELYGYN VPQVDYVPWS TSLEQYVNDG
1310 1320 1330 1340 1350
EHNDKESQHA LMPLYHFVTS DLPSNTKAPE LDDVNAATAL RADATWSGVD
1360 1370 1380 1390 1400
ASAGAGVTEE LVGLYASYLV QTGFLPAPTV AGARPLPAAQ ISEEQKKTLL
SVGGRGGTS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y13967 Genomic DNA Translation: CAA74300.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y13967 Genomic DNA Translation: CAA74300.1 |
3D structure databases
SMRi | O74298 |
ModBasei | Search... |
Proteomic databases
PRIDEi | O74298 |
Enzyme and pathway databases
UniPathwayi | UPA00033;UER00032 |
Family and domain databases
CDDi | cd05235, SDR_e1, 1 hit |
Gene3Di | 1.10.1200.10, 1 hit 3.30.300.30, 1 hit 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR001242, Condensatn IPR013120, Far_NAD-bd IPR014397, Lys2 IPR036291, NAD(P)-bd_dom_sf IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR010080, Thioester_reductase-like_dom |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF00668, Condensation, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 1 hit |
SMARTi | View protein in SMART SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit TIGR03443, alpha_am_amid, 1 hit TIGR01746, Thioester-redct, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LYS2_PENCH | |
Accessioni | O74298Primary (citable) accession number: O74298 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 27, 2004 |
Last sequence update: | November 1, 1998 | |
Last modified: | February 23, 2022 | |
This is version 103 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families