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Q12572

- LYS2_CANAX

UniProt

Q12572 - LYS2_CANAX

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Protein
L-aminoadipate-semialdehyde dehydrogenase large subunit
Gene
LYS2
Organism
Candida albicans (Yeast)
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

Binds 1 phosphopantetheine covalently Reviewed prediction.

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
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13911391L-aminoadipate-semialdehyde dehydrogenase large subunit
PRO_0000193149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei884 – 8841O-(pantetheine 4'-phosphoryl)serine Reviewed prediction

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ12572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini852 – 90251Acyl carrier
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3320.

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.

Q12572-1 [UniParc]FASTAAdd to Basket

« Hide

MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA     50
VFAALVYRLT GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE 100
YENNISQINY KALSEVSHRI KEAKGLDENP GLFRLSYQHA HSNQQLNTTV 150
EGSIRDLAIY TDGTKFTIYY NALLYSHERV VICGEQFAQL TTVSGDTDTV 200
IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN KHPDRTCVVE 250
TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD 300
LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ 350
LVVDYISNEL DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP 400
AGVIVGPDSR PTLSFTSGSE GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD 450
KFTILSGIAH DPIQRDMFTP LFLGAQLLVP TADDIGTPGK LADWMAKYGA 500
TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR LQSLAENVFI 550
VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV 600
NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW 650
IEQDEANKKS SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ 700
VKIRGFRIEL GEIDTHLSQH PLVRENVTLV RRDKNEEPTL ISYIVPKDSP 750
ELKTFFADVD FPLKKSNDPI VKGLVAYREL IKDIKGYLKK KLASYAIPTI 800
IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD AQAAEEENLT 850
KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE 900
IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK 950
ELSKSALLES YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD 1000
IKVYAHVRAS SKEAGLQRLR QTGITYGIWD ENWAEKIEIV LGDLSKEKFG 1050
LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ LRMLNVIGTI NVFNMAGEVK 1100
LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ GSAKGLGNGY 1150
GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG 1200
SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI 1250
LFNNFLGCLK AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD 1300
NLPQDTKAPE LDDSNAAKSL KQDSKYTGED FSAGKGVDLD QTGVYISYLI 1350
KIGFLPKPTG TGEKKLPEVE ISDESLKLIS GGAGARGSAA K 1391
Length:1,391
Mass (Da):154,741
Last modified:July 15, 1999 - v2
Checksum:iB7E641866235BCDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58133 Genomic DNA. Translation: AAC02241.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58133 Genomic DNA. Translation: AAC02241.1 .

3D structure databases

ProteinModelPortali Q12572.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3320.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 11651 / B792 / 171D.

Entry informationi

Entry nameiLYS2_CANAX
AccessioniPrimary (citable) accession number: Q12572
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 86 of the entry and version 2 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

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