Align Glutamyl-tRNA(Gln) amidotransferase subunit A; Glu-ADT subunit A; EC 6.3.5.7 (uncharacterized)
to candidate GFF2395 HP15_2343 amidase signature enzyme
Query= curated2:Q7UT33 (499 letters) >FitnessBrowser__Marino:GFF2395 Length = 495 Score = 196 bits (497), Expect = 2e-54 Identities = 160/499 (32%), Positives = 235/499 (47%), Gaps = 57/499 (11%) Query: 4 SASEILKQLDSGEVTAVEVIAQSLAAIRASQPTINAFTHVAEETAMQAAEAVDADRKAGK 63 SA ++LKQL++G +T+ + L IR PTINA + E+ A+ A D +R AG Sbjct: 12 SAHDLLKQLEAGTLTSEALTTALLERIREHNPTINAVVTLDEQKALTNARRADEERAAGS 71 Query: 64 TLGPLAGLPVAIKDVLCTSDMPTTCSSKMLEGFVPPYDATVVARLKSAGAIVVGKTNMDE 123 GPL GLP+ +KD + M T + L P A VV RL+ AGAI++GKTN+ Sbjct: 72 ARGPLHGLPLTLKDTWEVAGMTCTAGAPALRDHKPNRHADVVQRLEDAGAIILGKTNVPI 131 Query: 124 FAMGASTETSAMGVTGNPWDTTKTPGGSSGGAAAAVAAGAVPLSLGTDTGGSIRQPAAFC 183 +A + GVT NP + TPGGSSGGAAAA+AAG PL +G+D GSIR PA FC Sbjct: 132 YATDLQSYNKLFGVTNNPHNLAHTPGGSSGGAAAALAAGMTPLEVGSDLAGSIRTPAHFC 191 Query: 184 GITGLKPTYGRVSRYGLV------AFASSLDQAGPMGWSVDDVAIGLQAMAGYDPRDSTS 237 G+ G KPT VS G + L + GPM S D+ + + +AG P Sbjct: 192 GVFGHKPTRSLVSFRGHIPGPPGTQSRPDLVEGGPMARSAGDLELLMSVIAGPRP----- 246 Query: 238 VNAEVPDFTPAMAAEDVRGM---RIGVLREG----LDQDGISPAVRDALATAESVFREQG 290 AE ++ AMA ++ + R+G+ E +DQ+ + + + E+G Sbjct: 247 --AEERSWSLAMAPSELNSLDQARVGLWLEDPLCPIDQE-----LTEGYQNLGNALSERG 299 Query: 291 AEIVEVELP--HSKYWVPTYYVIAPCEASSNLSRFDGAHYGYRVADAEIAAADSGPLEAM 348 A + E P ++ +P Y+ + S++L + +A E GP+ Sbjct: 300 ALVTEARHPLLSLEHILPAYFNLLGALLSTSLKPAQRRQMKW-IARLEPWLKFLGPMTPF 358 Query: 349 YSLSRAGGFGSEVKRRIMVGTYALSEGYYDAYYNQALKVRRLIRNDYDAAFQQVDLMLGP 408 G +G V + + A SE +R +R + ++ FQ+VD++L P Sbjct: 359 -----IGEYGRGVNQPV-YQWMAWSE------------MREKMRAEIESLFQEVDVLLTP 400 Query: 409 VTPSPAFALNEK----------TDDPIAMYLCDLFTVGANLAGVPAISLPGGFDAVGLPV 458 VTP+ A + P A + A L G+PA S+P G GLP Sbjct: 401 VTPTTAIRHDHSHPVFKRRITVAGQPRAYMDQFCWIAFATLLGLPATSVPIGRTKEGLPF 460 Query: 459 GVQ-LQAPVMEETRLLRAG 476 VQ + AP M+ T + AG Sbjct: 461 NVQVIGAPGMDLTTIGFAG 479 Lambda K H 0.316 0.132 0.381 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: 584 Number of extensions: 30 Number of successful extensions: 4 Number of sequences better than 1.0e-02: 1 Number of HSP's gapped: 2 Number of HSP's successfully gapped: 2 Length of query: 499 Length of database: 495 Length adjustment: 34 Effective length of query: 465 Effective length of database: 461 Effective search space: 214365 Effective search space used: 214365 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 (21.6 bits) S2: 52 (24.6 bits)
This GapMind analysis is from Jul 25 2024. The underlying query database was built on Jul 25 2024.
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:
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