Gene_locus Report for: 9sphn-q3vck8Sphingopyxis alaskensis; Sphingopyxis sp.; S. fribergensis; S. macrogoltabida; S. granuli; S. terrae; Gammaproteobacteria bacterium; flava; S. macrogoltabidus hypothetical protein Comment Other strains: Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256); Sphingopyxis sp.; Sphingopyxis fribergensis; Sphingopyxis macrogoltabida; Sphingopyxis granuli; Sphingopyxis terrae NBRC 15098; Gammaproteobacteria bacterium; Sphingopyxis flava; Sphingomonas macrogoltabidus Relationship (Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Proteobacteria: N E > Alphaproteobacteria: N E > Sphingomonadales: N E > Sphingomonadaceae: N E > Sphingopyxis: N E > Sphingopyxis alaskensis: N E > Sphingopyxis alaskensis RB2256: N E
ACPH_Peptidase_S9 : sphal-q1gq33 Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) SpI-IsoP, Sala_2532, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases-like protein, 9sphn-q3vd53Sphingopyxis alaskensis RB2256 peptidase s9, prolyl oligopeptidase active site region precursor. AlphaBeta_hydrolase : 9sphn-q3vh72Sphingopyxis alaskensis RB2256 alpha/beta hydrolase fold. Carboxypeptidase_S10 : sphal-q1gwh9Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) peptidase s10, serine carboxypeptidase precursor. Dienelactone_hydrolase : 9sphn-q3v9g2Sphingopyxis alaskensis RB2256 carboxymethylenebutenolidase (EC 3.1.1.45), sphal-q1gp66Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) carboxymethylenebutenolidase (EC 3.1.1.45), sphal-q1gte3Sphingopyxis alaskensis RB2256 dienelactone hydrolase. Epoxide_hydrolase : 9sphn-q3vax0Sphingopyxis alaskensis RB2256 alpha/beta hydrolase fold:epoxide hydrolase, n-terminal precursor. Hormone-sensitive_lipase_like : 9sphn-q3vbc4Sphingopyxis alaskensis RB2256 esterase/lipase/thioesterase. Monoglyceridelipase_lysophospholip : sphal-q1gwq1Sphingopyxis alaskensis RB2256 acylglycerol lipase precursor (EC 3.1.1.23). PHA_synth_I : sphal-q1gvu6Sphingopyxis alaskensis (Sphingomonas alaskensis) poly(r)-hydroxyalkanoic acid synthase, class i. PHB_depolymerase_PhaZ : 9sphn-q3v955Sphingopyxis alaskensis RB2256 polyhydroxyalkanoate depolymerase precursor. Proline_iminopeptidase : 9sphn-q3vdj4Sphingopyxis alaskensis RB2256 alpha/beta hydrolase fold precursor. Prolyl_oligopeptidase_S9 : 9sphn-q3vew0Sphingopyxis alaskensis RB2256 peptidase s9, prolyl oligopeptidase active site region. S9N_PPCE_Peptidase_S9 : 9sphn-q3v961Sphingopyxis alaskensis RB2256 prolyl oligopeptidase precursor (EC 3.4.21.26). S9N_PREPL_Peptidase_S9 : 9sphn-q3vbq9Sphingopyxis alaskensis RB2256 oligopeptidase b (EC 3.4.21.83) Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)Sphingopyxis sp. LC81: N, E.
Sphingopyxis sp. LC363: N, E.
Sphingopyxis fribergensis: N, E.
Sphingopyxis sp. 113P3: N, E.
Sphingopyxis sp. C-1: N, E.
Sphingomonas macrogoltabidus: N, E.
Sphingopyxis macrogoltabida: N, E.
Sphingopyxis sp. Root1497: N, E.
Sphingopyxis sp. Root214: N, E.
Sphingopyxis sp. H115: N, E.
Sphingopyxis sp. H050: N, E.
Sphingopyxis sp. HIX: N, E.
Sphingopyxis sp. H038: N, E.
Sphingopyxis sp. H071: N, E.
Sphingopyxis sp. A083: N, E.
Sphingopyxis granuli: N, E.
Sphingopyxis terrae NBRC 15098: N, E.
Sphingopyxis terrae subsp. terrae NBRC 15098: N, E.
Sphingopyxis sp. SCN 67-31: N, E.
Gammaproteobacteria bacterium RIFCSPHIGHO2_12_FULL_63_22: N, E.
Sphingopyxis sp. RIFCSPHIGHO2_01_FULL_65_24: N, E.
Sphingopyxis sp. QXT-31: N, E.
Sphingopyxis sp. 65-8: N, E.
Sphingopyxis flava: N, E.
Sphingopyxis sp. MC1: N, E.
Molecular evidence | | Database | No mutation
No structure
No kinetic
No Substrate
No inhibitor
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>3 Genbank links 5 more: AAIP01000007, WP_037510410, WP_053553654<8 Genbank links 5 less: AAIP01000007, WP_037510410, WP_053553654, WP_054588059, WP_011541103, WP_058453864, WP_003044467, WP_067107735>3 UniProt links 21 more: A0A095B3X1, A0A095BKK5, A0A0A7PDY6<24 UniProt links 21 less: A0A095B3X1, A0A095BKK5, A0A0A7PDY6, A0A0M5IWX5, A0A0M9TYX8, A0A0P0DBI6, A0A0Q7YYB2, A0A0Q8RLN1, A0A0W1CUJ9, A0A0W1DUL0, A0A0W1EWD3, A0A0W1F132, A0A0W1GMJ3, A0A0W1IDU6, A0A109YMB5, A0A142W137, A0A1E4JR33, A0A1G0HYT4, A0A1G3KGB2, A0A1P8WUL1, A0A1Q3USM1, A0A1T4ZTB3, N9W1I9, Q1GV09>3 Interpro links 21 more: A0A095B3X1, A0A095BKK5, A0A0A7PDY6<24 Interpro links 21 less: A0A095B3X1, A0A095BKK5, A0A0A7PDY6, A0A0M5IWX5, A0A0M9TYX8, A0A0P0DBI6, A0A0Q7YYB2, A0A0Q8RLN1, A0A0W1CUJ9, A0A0W1DUL0, A0A0W1EWD3, A0A0W1F132, A0A0W1GMJ3, A0A0W1IDU6, A0A109YMB5, A0A142W137, A0A1E4JR33, A0A1G0HYT4, A0A1G3KGB2, A0A1P8WUL1, A0A1Q3USM1, A0A1T4ZTB3, N9W1I9, Q1GV09>3 Pfam links 21 more: A0A095B3X1, A0A095BKK5, A0A0A7PDY6<24 Pfam links 21 less: A0A095B3X1, A0A095BKK5, A0A0A7PDY6, A0A0M5IWX5, A0A0M9TYX8, A0A0P0DBI6, A0A0Q7YYB2, A0A0Q8RLN1, A0A0W1CUJ9, A0A0W1DUL0, A0A0W1EWD3, A0A0W1F132, A0A0W1GMJ3, A0A0W1IDU6, A0A109YMB5, A0A142W137, A0A1E4JR33, A0A1G0HYT4, A0A1G3KGB2, A0A1P8WUL1, A0A1Q3USM1, A0A1T4ZTB3, N9W1I9, Q1GV09>3 PIRSF links 21 more: A0A095B3X1, A0A095BKK5, A0A0A7PDY6<24 PIRSF links 21 less: A0A095B3X1, A0A095BKK5, A0A0A7PDY6, A0A0M5IWX5, A0A0M9TYX8, A0A0P0DBI6, A0A0Q7YYB2, A0A0Q8RLN1, A0A0W1CUJ9, A0A0W1DUL0, A0A0W1EWD3, A0A0W1F132, A0A0W1GMJ3, A0A0W1IDU6, A0A109YMB5, A0A142W137, A0A1E4JR33, A0A1G0HYT4, A0A1G3KGB2, A0A1P8WUL1, A0A1Q3USM1, A0A1T4ZTB3, N9W1I9, Q1GV09>3 SUPERFAM links 21 more: A0A095B3X1, A0A095BKK5, A0A0A7PDY6<24 SUPERFAM links 21 less: A0A095B3X1, A0A095BKK5, A0A0A7PDY6, A0A0M5IWX5, A0A0M9TYX8, A0A0P0DBI6, A0A0Q7YYB2, A0A0Q8RLN1, A0A0W1CUJ9, A0A0W1DUL0, A0A0W1EWD3, A0A0W1F132, A0A0W1GMJ3, A0A0W1IDU6, A0A109YMB5, A0A142W137, A0A1E4JR33, A0A1G0HYT4, A0A1G3KGB2, A0A1P8WUL1, A0A1Q3USM1, A0A1T4ZTB3, N9W1I9, Q1GV09
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Sequence Graphical view for this peptide sequence: 9sphn-q3vck8
Colored MSA for Atu1826-like (raw)
MPDVIFPGPEGRIEGRFSPPPRPRAPVALILHPHPQGGGTMNDRITQAMY
KSFVARGFAVLRFNFRGVGRSQGTFDNGIGELSDAASALDWVQSIHPEAQ
TTWVAGFSFGAWIGMQLLMRRPEIRGFLSVAPPANMYDFSFLAPCPSSGI
IVAGGQDEIVPPSAVQKLVDKLRTQKGITIHHDEIPRANHFFEHELDQLM
KSLDNYLDMRLAPDSPIR
Legend
This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA
MPDVIFPGPEGRIEGRFSPPPRPRAPVALILHPHPQGGGTMNDRITQAMY
KSFVARGFAVLRFNFRGVGRSQGTFDNGIGELSDAASALDWVQSIHPEAQ
TTWVAGFSFGAWIGMQLLMRRPEIRGFLSVAPPANMYDFSFLAPCPSSGI
IVAGGQDEIVPPSAVQKLVDKLRTQKGITIHHDEIPRANHFFEHELDQLM
KSLDNYLDMRLAPDSPIR
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