Unreviewed, UniProtKB/TrEMBL A1ZA78 (A1ZA78_DROME)

Names and origin

Protein names

Submitted name:
    ATP citrate lyase, isoform A EMBL AAF58082.1
    EC=2.3.3.8
    EC=6.2.1.5

Gene names

Name:	ATPCL FlyBase FBgn0020236
ORF Names:	Dmel_CG8322 EMBL AAF58082.1

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1086 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Molecular function	Acyltransferase Ligase Lyase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	lipid particle Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATP citrate synthase activity Inferred from electronic annotation. Source: InterPro acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A1ZA78-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: C2ADB2C4F517A731	FASTA	1,086	118,591
	10 20 30 40 50 60 MSAKAITEAS GKDILNRHLN THGAGAATCR FSTVNSTTDW SKLAVDHPWL LTTPLVCKPD 70 80 90 100 110 120 QLIKRRGKLG LIGVKKNFEQ VKQWIGERLN KDQKIGNAVG KLRNFIIEPF VPHTDAEEMY 130 140 150 160 170 180 VCIYSHRAAD TILFYHQGGV DIGDVDAKAV KLDVPVNSSL SLADVKSKLL KEVKDAGTKE 190 200 210 220 230 240 RIAKFVSALY TTYVDLYFTY LEINPLVVTA DNLYILDLAA KLDSTADFIC RPKWGEIDYP 250 260 270 280 290 300 PPFGRDAYPE EAYIADLDAK SGASLKLTIL NRNGRIWTMV AGGGASVIYS DTICDLGGAS 310 320 330 340 350 360 ELANYGEYSG APSEQQTYEY AKTILNLMTS SPKHPDGKVL ITGGGIANFT NVAATFQGII 370 380 390 400 410 420 TALREFQPKL VEHNVSIFVR RAGPNYQEGL RKMRDFGSTL GIPLHVFGPE THMTAICGMA 430 440 450 460 470 480 LGKRPIPQTA SVEFSTANFL LPGGQQAQAD LKAASDASEA LGSGSADEAD SAGISGAQRN 490 500 510 520 530 540 GSSLNRKFFS NTTKAIVWGM QQRAVQRDEP SVVAMVYPFT GDHKQKYYWG HKEILIPVYK 550 560 570 580 590 600 KMSDAIHKHK EVDVMVNFAS MRSAYESTLE VLEFPQIRTV AIIAEGIPEN MTRKLIIEAD 610 620 630 640 650 660 KKGVAIIGPA TVGGVKPGCF KIGNTGGMLD NILHSKLYRP GSVAYVSRSG GMSNELNNII 670 680 690 700 710 720 SKATDGVIEG IAIGGDRYPG STFMDHILRY QADPETKLIV LLGEVGGTEE YDVCAALKDG 730 740 750 760 770 780 RITKPLVAWC IGTCASMFTS EVQFGHAGSC ANSDRETATA KNKGLRDAGA YVPDSFDTLG 790 800 810 820 830 840 ELIHHVYGEL VKTGRVVPKE EVPPPTVPMD YSWARELGLI RKPASFMTSI CDERGQELIY 850 860 870 880 890 900 AGMPISEVLS KDVGIGGVIS LLWFQRCLPS YVCKFFEMCL MVTADHGPAV SGAHNTIVCA 910 920 930 940 950 960 RAGKDLVSSV VSGLLTIGDR FGGALDGSAR QFSEAYDTNL HPMEFVNKMR KEGKLILGIG 970 980 990 1000 1010 1020 HRVKSINNPD VRVKIIKEFV LENFPACPLL KYALEVEKIT TNKKPNLILN VDGVIATAFV 1030 1040 1050 1060 1070 1080 DMLRNSGSFT SEEAQEYINV GAINSLFVLG RSIGFIGHYM DQKRLKQGLY RHPWDDISYV IPEQYN

References

[1]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF58082.1.
RefSeq	NP_523755.1. NP_725514.1.
UniGene	Dm.3204
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	A1ZA78.
Genome annotation databases
Ensembl	FBgn0020236. Drosophila melanogaster. [Contig view]
GeneID	36760.
KEGG	dme:Dmel_CG8322.
Organism-specific databases
FlyBase	FBgn0020236. ATPCL.
Phylogenomic databases
OMA	A1ZA78. IVSAPHA.
Family and domain databases
InterPro	IPR014608. ATP-citrate_synthase. IPR013650. ATP-grasp_succ-CoA_synth-type. IPR013816. ATP_grasp_subdomain_2. IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016143. Citrate_synth-like_sm_a-sub. IPR003781. CoA_bd. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR017866. Succ-CoA_synthase_bsu_CS. IPR016102. Succinyl-CoA_synth-like. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:1.10.230.10. Citrate_synthase_sm_a-sub. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
Pfam	PF08442. ATP-grasp_2. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF036511. ATP_citrt_syn. 1 hit.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. PS01217. SUCCINYL_COA_LIG_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	800244.

Entry information

Entry name

A1ZA78_DROME

Accession

Primary (citable) accession number: A1ZA78

Entry history

Integrated into UniProtKB/TrEMBL:	February 6, 2007
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)