Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12572

- LYS2_CANAX

UniProt

Q12572 - LYS2_CANAX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.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
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13911391L-aminoadipate-semialdehyde dehydrogenase large subunitPRO_0000193149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei884 – 8841O-(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

ProteinModelPortaliQ12572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini852 – 90251Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA
60 70 80 90 100
VFAALVYRLT GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE
110 120 130 140 150
YENNISQINY KALSEVSHRI KEAKGLDENP GLFRLSYQHA HSNQQLNTTV
160 170 180 190 200
EGSIRDLAIY TDGTKFTIYY NALLYSHERV VICGEQFAQL TTVSGDTDTV
210 220 230 240 250
IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN KHPDRTCVVE
260 270 280 290 300
TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD
310 320 330 340 350
LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ
360 370 380 390 400
LVVDYISNEL DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP
410 420 430 440 450
AGVIVGPDSR PTLSFTSGSE GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD
460 470 480 490 500
KFTILSGIAH DPIQRDMFTP LFLGAQLLVP TADDIGTPGK LADWMAKYGA
510 520 530 540 550
TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR LQSLAENVFI
560 570 580 590 600
VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV
610 620 630 640 650
NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW
660 670 680 690 700
IEQDEANKKS SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ
710 720 730 740 750
VKIRGFRIEL GEIDTHLSQH PLVRENVTLV RRDKNEEPTL ISYIVPKDSP
760 770 780 790 800
ELKTFFADVD FPLKKSNDPI VKGLVAYREL IKDIKGYLKK KLASYAIPTI
810 820 830 840 850
IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD AQAAEEENLT
860 870 880 890 900
KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE
910 920 930 940 950
IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK
960 970 980 990 1000
ELSKSALLES YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD
1010 1020 1030 1040 1050
IKVYAHVRAS SKEAGLQRLR QTGITYGIWD ENWAEKIEIV LGDLSKEKFG
1060 1070 1080 1090 1100
LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ LRMLNVIGTI NVFNMAGEVK
1110 1120 1130 1140 1150
LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ GSAKGLGNGY
1160 1170 1180 1190 1200
GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG
1210 1220 1230 1240 1250
SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI
1260 1270 1280 1290 1300
LFNNFLGCLK AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD
1310 1320 1330 1340 1350
NLPQDTKAPE LDDSNAAKSL KQDSKYTGED FSAGKGVDLD QTGVYISYLI
1360 1370 1380 1390
KIGFLPKPTG TGEKKLPEVE ISDESLKLIS GGAGARGSAA K
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: October 29, 2014
This is version 88 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