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O74298

- LYS2_PENCH

UniProt

O74298 - LYS2_PENCH

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Protein

L-aminoadipate-semialdehyde dehydrogenase large subunit

Gene

lys2

Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH.

Catalytic activityi

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 1 phosphopantetheine covalently.Curated

Pathwayi

GO - Molecular functioni

  1. L-aminoadipate-semialdehyde dehydrogenase activity Source: UniProtKB-EC
  2. phosphopantetheine binding Source: InterPro

GO - Biological processi

  1. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00033; UER00032.

Names & Taxonomyi

Protein namesi
Recommended name:
L-aminoadipate-semialdehyde dehydrogenase large subunit (EC:1.2.1.31)
Alternative name(s):
Alpha-aminoadipate reductase
Short name:
Alpha-AR
Gene namesi
Name:lys2
OrganismiPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifieri5076 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14091409L-aminoadipate-semialdehyde dehydrogenase large subunitPRO_0000193151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei896 – 8961O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Structurei

3D structure databases

ProteinModelPortaliO74298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini863 – 93472Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR014397. L-NH2adipate-semiAld_DH_lsu.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR010080. Thioester_reductase-like_dom.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001617. Alpha-AR. 1 hit.
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR03443. alpha_am_amid. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74298-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:1,409
Mass (Da):154,842
Last modified:November 1, 1998 - v1
Checksum:iA85DFD397BAB29AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13967 Genomic DNA. Translation: CAA74300.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13967 Genomic DNA. Translation: CAA74300.1 .

3D structure databases

ProteinModelPortali O74298.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00033 ; UER00032 .

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR014397. L-NH2adipate-semiAld_DH_lsu.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR010080. Thioester_reductase-like_dom.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view ]
PIRSFi PIRSF001617. Alpha-AR. 1 hit.
SUPFAMi SSF47336. SSF47336. 1 hit.
TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
TIGR03443. alpha_am_amid. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of the lys2 gene of Penicillium chrysogenum encoding alpha-aminoadipic acid reductase."
    Casqueiro J., Gutierrez S., Banuelos O., Fierro F., Velasco J., Martin J.F.
    Mol. Gen. Genet. 259:549-556(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: AS-P-78.

Entry informationi

Entry nameiLYS2_PENCH
AccessioniPrimary (citable) accession number: O74298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3