| Tag | Content |
|---|
| CPLM ID | CPLM-002767 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aconitate hydratase |
Protein Synonyms/Alias | Aconitase; Citrate hydro-lyase |
Gene Name | citB |
Gene Synonyms/Alias | BSU18000 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 67 | VDGFVIKKEHVENLA | acetylation | [1] | | 89 | KDIDVPFKPSRVILQ | acetylation | [1] | | 402 | SAMQETFKKQLVSPA | acetylation | [1] | | 423 | LNAEEENKEIKFKLL | acetylation | [1] | | 592 | TDPIGVGKDGQNVYF | acetylation | [1] | | 701 | SPAGAIGKDTPAGKY | acetylation | [1] | | 786 | GLVVLAGKDYGMGSS | acetylation | [1] |
|
Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). |
Sequence Annotation | METAL 450 450 Iron-sulfur (4Fe-4S) (By similarity).
METAL 516 516 Iron-sulfur (4Fe-4S) (By similarity).
METAL 519 519 Iron-sulfur (4Fe-4S) (By similarity). |
Keyword | Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; Tricarboxylic acid cycle. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 909 AA |
Protein Sequence | MANEQKTAAK DVFQARKTFT TNGKTYHYYS LKALEDSGIG KVSKLPYSIK VLLESVLRQV 60
DGFVIKKEHV ENLAKWGTAE LKDIDVPFKP SRVILQDFTG VPAVVDLASL RKAMAAVGGD 120
PDKINPEIPV DLVIDHSVQV DKAGTEDALA VNMDLEFERN AERYKFLSWA KKAFNNYQAV 180
PPATGIVHQV NLEFLASVVH AIEEDGELVT YPDTLVGTDS HTTMINGIGV LGWGVGGIEA 240
EAGMLGQPSY FPVPEVIGAK LVGKLPNGTT ATDLALKVTQ VLREKGVVGK FVEFFGPGIA 300
ELPLADRATI ANMAPEYGAT CGFFPVDEEA LNYLRLTGRD PEHIDVVEAY CRSNGLFYTP 360
DAEDPQFTDV VEIDLSQIEA NLSGPKRPQD LIPLSAMQET FKKQLVSPAG NQGFGLNAEE 420
ENKEIKFKLL NGEETVMKTG AIAIAAITSC TNTSNPYVLI GAGLVAKKAV ELGLKVPNYV 480
KTSLAPGSKV VTGYLVNSGL LPYMKELGFN LVGYGCTTCI GNSGPLSPEI EEAVAKNDLL 540
ITSVLSGNRN FEGRIHPLVK GNYLASPPLV VAYALAGTVN INLKTDPIGV GKDGQNVYFN 600
DIWPSMDEIN ALVKQTVTPE LFRKEYETVF DDNKRWNEIE TTDEALYKWD NDSTYIQNPP 660
FFEEMSVEPG KVEPLKGLRV VGKFGDSVTT DHISPAGAIG KDTPAGKYLQ EKGVSPRDFN 720
SYGSRRGNHE VMMRGTFANI RIKNQIAPGT EGGFTTYWPT GEVTSIYDAC MKYKEDKTGL 780
VVLAGKDYGM GSSRDWAAKG TNLLGIRTVI AESFERIHRS NLVFMGVLPL QFKQGENADT 840
LGLTGKEVIE VDVDETVRPR DLVTVRAINE DGNVTTFEAV VRFDSEVEID YYRHGGILQM 900
VLREKMKQS 909 |
Gene Ontology | GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. 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-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |