| Tag | Content |
|---|
| CPLM ID | CPLM-007153 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable aconitate hydratase 2 |
Protein Synonyms/Alias | Aconitase; Citrate hydro-lyase |
Gene Name | ACO2 |
Gene Synonyms/Alias | YJL200C; J0327 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 545 | GFEHGRDKFYPEMDP | acetylation | [1] | | 590 | LKTNVLLKVEGKCTT | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). |
Sequence Annotation | REGION 189 191 Substrate binding (By similarity).
REGION 672 673 Substrate binding (By similarity).
METAL 385 385 Iron-sulfur (4Fe-4S) (By similarity).
METAL 448 448 Iron-sulfur (4Fe-4S) (By similarity).
METAL 451 451 Iron-sulfur (4Fe-4S) (By similarity).
BINDING 96 96 Substrate (By similarity).
BINDING 476 476 Substrate (By similarity).
BINDING 481 481 Substrate (By similarity). |
Keyword | 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; Tricarboxylic acid cycle. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 789 AA |
Protein Sequence | MLSSANRFYI KRHLATHANM FPSVSKNFQT KVPPYAKLLT NLDKIKQITN NAPLTLAEKI 60
LYSHLCDPEE SITSSDLSTI RGNKYLKLNP DRVAMQDASA QMALLQFMTT GLNQTSVPAS 120
IHCDHLIVGK DGETKDLPSS IATNQEVFDF LESCAKRYGI QFWGPGSGII HQIVLENFSA 180
PGLMMLGTDS HTPNAGGLGA IAIGVGGADA VDALTGTPWE LKAPKILGVK LTGKLNGWST 240
PKDVITKLAG LLTVRGGTGY IVEYFGEGVS TLSCTGMATI CNMGAEIGAT TSTFPYQEAH 300
KRYLQATNRA EVAEAADVAL NKFNFLRADK DAQYDKVIEI DLSAIEPHVN GPFTPDLSTP 360
ISQYAEKSLK ENWPQKVSAG LIGSCTNSSY QDMSRVVDLV KQASKAGLKP RIPFFVTPGS 420
EQIRATLERD GIIDIFQENG AKVLANACGP CIGQWNREDV SKTSKETNTI FTSFNRNFRA 480
RNDGNRNTMN FLTSPEIVTA MSYSGDAQFN PLTDSIKLPN GKDFKFQPPK GDELPKRGFE 540
HGRDKFYPEM DPKPDSNVEI KVDPNSDRLQ LLEPFKPWNG KELKTNVLLK VEGKCTTDHI 600
SAAGVWLKYK GHLENISYNT LIGAQNKETG EVNKAYDLDG TEYDIPGLMM KWKSDGRPWT 660
VIAEHNYGEG SAREHAALSP RFLGGEILLV KSFARIHETN LKKQGVLPLT FANESDYDKI 720
SSGDVLETLN LVDMIAKDGN NGGEIDVKIT KPNGESFTIK AKHTMSKDQI DFFKAGSAIN 780
YIGNIRRNE 789 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:SGD. GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0003994; F:aconitate hydratase activity; ISS:SGD. GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |