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Protein

Aspartate aminotransferase

Gene

Dere\GG24563

Organism
Drosophila erecta (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AminotransferaseUniRule annotationImported, Transferase

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferaseUniRule annotation (EC:2.6.1.1UniRule annotation)
Gene namesi
Name:Dere\GG24563Imported
ORF Names:Dere_GG24563Imported, GG24563Imported
OrganismiDrosophila erecta (Fruit fly)Imported
Taxonomic identifieri7220 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000008711 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0116695. Dere\GG24563.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB3N8Z8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 419368Aminotran_1_2InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

KOiK14455.
OMAiSWANHAA.
OrthoDBiEOG74J980.
PhylomeDBiB3N8Z8.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B3N8Z8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQICKRGLL ISNRLAPAAL RCKSTWFSEV QMGPPDAILG VTEAFKKDTN
60 70 80 90 100
PKKINLGAGA YRDDNTQPFV LPSVREAENR VLSRKLDKEY ATIIGLPEFY
110 120 130 140 150
NKAIELALGK GSKRLAAKHN VTAQSISGTG ALRIGAAFLA KFWKGNREIY
160 170 180 190 200
IPSPSWGNHV AIFEHAGLPV NRYRYYDKDT CALDFSGLIE DLKKIPEKSI
210 220 230 240 250
VLLHACAHNP TGVDPTLEQW REISALVKKR NLYPFIDMAY QGFATGDIDR
260 270 280 290 300
DAQAVRTFEA DGHDFCLAQS FAKNMGLYGE RAGAFTVLCS DEEEAARVMS
310 320 330 340 350
QVKILIRGLY SNPPVHGARI AAEILNNEDL RAQWLKDVKL MADRIIDVRT
360 370 380 390 400
KLKDNLIKLG SSQNWDHIVN QIGMFCFTGL KPEQVQKLIK DHSVYLTNDG
410 420
RVSMAGVTSK NVEYLAESIH KVTK
Length:424
Mass (Da):47,256
Last modified:September 2, 2008 - v1
Checksum:i31F6BD463874EA29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH954177 Genomic DNA. Translation: EDV57398.1.
RefSeqiXP_001968339.1. XM_001968303.2.

Genome annotation databases

EnsemblMetazoaiFBtr0144617; FBpp0143109; FBgn0116695.
GeneIDi6541450.
KEGGider:Dere_GG24563.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH954177 Genomic DNA. Translation: EDV57398.1.
RefSeqiXP_001968339.1. XM_001968303.2.

3D structure databases

ProteinModelPortaliB3N8Z8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0144617; FBpp0143109; FBgn0116695.
GeneIDi6541450.
KEGGider:Dere_GG24563.

Organism-specific databases

FlyBaseiFBgn0116695. Dere\GG24563.

Phylogenomic databases

KOiK14455.
OMAiSWANHAA.
OrthoDBiEOG74J980.
PhylomeDBiB3N8Z8.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evolution of genes and genomes on the Drosophila phylogeny."
    Drosophila 12 Genomes Consortium
    Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.
    , Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.
    Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tucson 14021-0224.01Imported.

Entry informationi

Entry nameiB3N8Z8_DROER
AccessioniPrimary (citable) accession number: B3N8Z8
Entry historyi
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.