Align aspartate transaminase (EC 2.6.1.1); glutamate-prephenate aminotransferase (EC 2.6.1.79) (characterized)
to candidate Ac3H11_1602 Aspartate aminotransferase (EC 2.6.1.1)
Query= BRENDA::Q02635 (400 letters) >lcl|FitnessBrowser__acidovorax_3H11:Ac3H11_1602 Aspartate aminotransferase (EC 2.6.1.1) Length = 408 Score = 434 bits (1117), Expect = e-126 Identities = 215/394 (54%), Positives = 271/394 (68%) Query: 5 ADALSRVKPSATIAVSQKARELKAKGRDVIGLGAGEPDFDTPDNIKKAAIDAIDRGETKY 64 AD L + S + ++Q+A +LK +G+ VI LG GEPDFDTP +I +AA A+ RGET Y Sbjct: 13 ADRLGAIGVSEIVRLTQEANQLKRQGQPVIVLGLGEPDFDTPAHILEAAQQAMARGETHY 72 Query: 65 TPVSGIPELREAIAKKFKRENNLDYTAAQTIVGTGGKQILFNAFMATLNPGDEVVIPAPY 124 T + G EL+ AI KFK N LD+ + G G KQIL+NA MA++NPGDEV++PAPY Sbjct: 73 TVLDGTAELKAAIQHKFKHYNGLDFQLNEITAGAGAKQILYNALMASVNPGDEVILPAPY 132 Query: 125 WVSYPEMVALCGGTPVFVPTRQENNFKLKAEDLDRAITPKTKWFVFNSPSNPSGAAYSHE 184 W SY +MV + GG PV VP + N F++ E L+ AITP+T+W NSPSNPSGAAYS E Sbjct: 133 WTSYADMVLIAGGVPVVVPCTEANGFRITPEQLEAAITPRTRWVFINSPSNPSGAAYSAE 192 Query: 185 ELKALTDVLMKHPHVWVLTDDMYEHLTYGDFRFATPVEVEPGLYERTLTMNGVSKAYAMT 244 +L+ + +V+ +HP VW+L DD+YEH+ Y FATP V P L +RTLT+NGVSKAYAMT Sbjct: 193 QLRPVLEVVERHPQVWLLADDIYEHILYDGRAFATPAAVLPSLRDRTLTVNGVSKAYAMT 252 Query: 245 GWRIGYAAGPLHLIKAMDMIQGQQTSGAASIAQWAAVEALNGPQDFIGRNKEIFQGRRDL 304 GWR+GY AGP LI AM ++Q Q TS +SI+Q AAV AL GPQD + + FQ RRDL Sbjct: 253 GWRLGYGAGPKALIAAMAVVQSQATSCPSSISQAAAVAALTGPQDVVRERCQAFQDRRDL 312 Query: 305 VVSMLNQAKGISCPTPEGAFYVYPSCAGLIGKTAPSGKVIETDEDFVSELLETEGVAVVH 364 VV+ LN + G+ C PEGAFY + SC G +G+T P G ++ TD DF + LL VAVV Sbjct: 313 VVAALNVSPGLRCRVPEGAFYTFASCEGALGRTTPGGLLLRTDADFCAYLLREHHVAVVP 372 Query: 365 GSAFGLGPNFRISYATSEALLEEACRRIQRFCAA 398 G GL P FRISYA S A L+EAC RIQR C A Sbjct: 373 GGVLGLAPYFRISYAASTADLQEACARIQRACQA 406 Lambda K H 0.318 0.134 0.402 Gapped Lambda K H 0.267 0.0410 0.140 Matrix: BLOSUM62 Gap Penalties: Existence: 11, Extension: 1 Number of Sequences: 1 Number of Hits to DB: 502 Number of extensions: 15 Number of successful extensions: 1 Number of sequences better than 1.0e-02: 1 Number of HSP's gapped: 1 Number of HSP's successfully gapped: 1 Length of query: 400 Length of database: 408 Length adjustment: 31 Effective length of query: 369 Effective length of database: 377 Effective search space: 139113 Effective search space used: 139113 Neighboring words threshold: 11 Window for multiple hits: 40 X1: 16 ( 7.3 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.7 bits) S2: 50 (23.9 bits)
This GapMind analysis is from Aug 03 2021. The underlying query database was built on Aug 03 2021.
Each pathway is defined by a set of rules based on individual steps or genes. Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam). Ublast hits may be split across two different proteins.
A candidate for a step is "high confidence" if either:
Otherwise, a candidate is "medium confidence" if either:
Other blast hits with at least 50% coverage are "low confidence."
Steps with no high- or medium-confidence candidates may be considered "gaps." For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. Gaps may be due to:
GapMind relies on the predicted proteins in the genome and does not search the six-frame translation. In most cases, you can search the six-frame translation by clicking on links to Curated BLAST for each step definition (in the per-step page).
For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code, or see changes to Amino acid biosynthesis since the publication.
If you notice any errors or omissions in the step descriptions, or any questionable results, please let us know
by Morgan Price, Arkin group, Lawrence Berkeley National Laboratory