LemaA.01471.b: aspartate aminotransferase, putative
Target Characteristics
| from organism: | Leishmania major Friedlin |
| most recent status: | in PDB |
| center reference id: | LemaA.01471.b |
| is community request: | True |
| associated disease: | Cutaneous leishmaniasis |
| NIH risk group: | 2 |
| is select agent: | False |
| NIH priority pathogens category: |
unclassified |
Ordering Clones & Proteins
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Clones*
| CENTER REFERENCE ID |
DOMAIN/REGION DESCRIPTION |
INFO | AA START |
AA STOP |
ORDER MATERIAL |
|---|---|---|---|---|---|
| LemaA.01471.b.B1.GE34449 | full length | 1 | 412 | GE34449 |
* SSGCID clones represent un-induced expression constructs which have been verified by sequencing from vector primers. Clones may contain a tag, such as N-term 6xHis. Get sequence information
using the button in the "info" column.
Proteins
| CENTER REFERENCE ID |
DOMAIN/REGION DESCRIPTION |
INFO | AA START |
AA STOP |
ORDER MATERIAL |
|---|---|---|---|---|---|
| LemaA.01471.b.B1.PW35059 | full length | 1 | 412 |
Structures
4H51
Deposited: 9/18/2012
Determination: XRay
Diffraction Image
Clone: LemaA.01471.b.B1.GE34449
Protein: LemaA.01471.b.B1.PW35059
Publications by SSGCID
Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.
Abendroth J, Choi R, Clifton MC, Edwards TE, Lorimer DD, Lukacs CM, Myler P, Staker BL, van Voorhis W, Wall A
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. - 2015
volume 71, issue Pt 5, pages 566-71
PMID: 25945710; PMCID: PMC4427166
External Resources
| Resource | Reference ID |
|---|---|
| EuPathDB: | TritrypDB:LmjF35.0820 |
| OrthoMCL: | OG5_126737 |
| RefSeq: | XP_843191.1 |
| UniProt: | Q4FX34 |
Enzyme & Pathway Information
| Pathway | Pathway ID | EC Number |
|---|---|---|
| superpathway of chorismate metabolism | ALL-CHORISMATE-PWY | 2.6.1.1 |
| L-phenylalanine degradation II (anaerobic) | ANAPHENOXI-PWY | 2.6.1.1 |
| L-asparagine degradation III (mammalian) | ASPARAGINE-DEG1-PWY-1 | 2.6.1.1 |
| L-aspartate degradation I | ASPARTATE-DEG1-PWY | 2.6.1.1 |
| L-aspartate biosynthesis | ASPARTATESYN-PWY | 2.6.1.1 |
| superpathway of L-aspartate and L-asparagine biosynthesis | ASPASN-PWY | 2.6.1.1 |
| anaerobic aromatic compound degradation (Thauera aromatica) | BENZCOA-PWY | 2.6.1.1 |
| superpathway of aromatic amino acid biosynthesis | COMPLETE-ARO-PWY | 2.6.1.1 |
| L-cysteine degradation I | CYSTEINE-DEG-PWY | 2.6.1.1 |
| L-glutamate degradation II | GLUTDEG-PWY | 2.6.1.1 |
| L-aspartate degradation II | MALATE-ASPARTATE-SHUTTLE-PWY | 2.6.1.1 |
| superpathway of L-lysine, L-threonine and L-methionine biosynthesis I | P4-PWY | 2.6.1.1 |
| L-phenylalanine biosynthesis I | PHESYN | 2.6.1.1 |
| aspartate superpathway | PWY0-781 | 2.6.1.1 |
| superpathway of L-isoleucine biosynthesis I | PWY-3001 | 2.6.1.1 |
| L-phenylalanine degradation III | PWY-5079 | 2.6.1.1 |
| superpathway of L-methionine biosynthesis (by sulfhydrylation) | PWY-5345 | 2.6.1.1 |
| superpathway of L-methionine biosynthesis (transsulfuration) | PWY-5347 | 2.6.1.1 |
| partial TCA cycle (obligate autotrophs) | PWY-5913 | 2.6.1.1 |
| Methanobacterium thermoautotrophicum biosynthetic metabolism | PWY-6146 | 2.6.1.1 |
| L-phenylalanine degradation IV (mammalian, via side chain) | PWY-6318 | 2.6.1.1 |
| superpathway of L-phenylalanine biosynthesis | PWY-6628 | 2.6.1.1 |
| sulfolactate degradation III | PWY-6638 | 2.6.1.1 |
| superpathway of sulfolactate degradation | PWY-6641 | 2.6.1.1 |
| (R)-cysteate degradation | PWY-6642 | 2.6.1.1 |
| coenzyme M biosynthesis II | PWY-6643 | 2.6.1.1 |
| C4 photosynthetic carbon assimilation cycle, NAD-ME type | PWY-7115 | 2.6.1.1 |
| C4 photosynthetic carbon assimilation cycle, PEPCK type | PWY-7117 | 2.6.1.1 |
| anaerobic energy metabolism (invertebrates, cytosol) | PWY-7383 | 2.6.1.1 |
| superpathway of anaerobic energy metabolism (invertebrates) | PWY-7389 | 2.6.1.1 |
| superpathway of L-threonine biosynthesis | THRESYN-PWY | 2.6.1.1 |
Sequences
These sequences are the native gene sequence; sequences of constructs derived from these sequences may differ due to codon optimization or other protocols.
To find the specific sequence of any material you may have ordered, click on the "more" button next to the name of that material.
AA Sequence
MSTQAAMTTA ERWQKIQAQA PDVIFDLAKR AAAAKGPKAN LVIGAYRDEQ GRPYPLRVVR KAEQLLLDMN LDYEYLPISG YQPFIDEAVK IIYGNTVELE NLVAVQTLSG TGAVSLGAKL LTRVFDAETT PIYLSDPTWP NHYGVVKAAG WKNICTYAYY DPKTVSLNFE GMKKDILAAP DGSVFILHQC AHNPTGVDPS QEQWNEIASL MLAKHHQVFF DSAYQGYASG SLDTDAYAAR LFARRGIEVL LAQSFSKNMG LYSERAGTLS LLLKDKTKRA DVKSVMDSLI REEYTCPPAH GARLAHLILS NNELRKEWEA ELSAMAERIR TMRRTVYDEL LRLQTPGSWE HVINQIGMFS FLGLSKAQCE YCQNHNIFIT VSGRANMAGL THETALMLAQ TINDAVRNVN RE
NT Sequence
atgtccacgc aggcggccat gaccacggcg gagcgctggc agaagattca ggcacaagct cccgatgtca tcttcgatct cgcaaaacgc gccgccgctg ccaagggccc caaggccaac ctcgtcattg gtgcctaccg cgacgagcag ggccgtccct atccgctacg cgtggtccgc aaggctgagc agcttctctt ggacatgaat ctcgactacg agtacctacc catctcgggc taccagccct tcatcgatga ggcggtaaag attatctacg gcaataccgt cgagctggag aacctggttg cggtgcagac gctgagcggg accggtgctg tctctctcgg ggcgaagctg ctgactcgcg tcttcgacgc tgagacgacg cccatctacc tttccgaccc cacgtggccc aaccactacg gcgtcgtgaa ggctgctggc tggaagaaca tctgcacgta cgcctactac gaccccaaga cggtcagcct gaatttcgag ggcatgaaga aagacattct ggcggcgccg gacggctccg tgttcattct gcaccagtgc gcgcacaacc ccaccggcgt ggacccgtcg caggagcagt ggaacgagat cgcgtcactg atgctggcca agcaccatca ggtgttcttc gactccgcct accaaggcta tgcgagcggc agcctcgaca cggacgcgta tgctgcccgc ctgtttgccc gccgcggcat cgaggtactg ctggcgcagt cgttctccaa gaacatgggc ttgtacagcg agcgtgcagg cacgctgtcg ctgctcctca aggacaagac gaagcgcgcg gatgtaaaga gcgtgatgga ttcgctgatc cgtgaggagt acacgtgccc cccagcccac ggtgcccgct tagcccacct aatcctgagc aacaacgaac tgcgaaagga gtgggaggca gagctatcag ccatggcaga gcgcatccgt acgatgcgcc gcaccgtgta cgacgagctg ctgcgcctgc agacgcccgg gagctgggaa catgtcatta accagattgg catgttttcc ttcctcgggc tgtcaaaggc gcagtgcgaa tactgccaaa accacaacat cttcatcaca gtgtcgggcc gcgctaacat ggcaggtctg acgcatgaga cggcgctgat gctagcacag acgatcaacg atgctgtgcg caatgtgaat cgtgagtga