| ProGlyProt ID | BC154 |
| Organism Information |
| Organism Name | Mycobacterium tuberculosis H37Rv |
| Domain | Bacteria |
| Classification | Family: Mycobacteriaceae
Suborder: Corynebacterineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria" |
| Taxonomic ID (NCBI) | 1773 |
| Genome Sequence (s) |
| GeneBank | BX842573.1 |
| EMBL | BX842573 |
| Gene Information |
| Gene Name | sodC (Rv0432) |
| NCBI Gene ID | 886358 |
| GenBank Gene Sequence | 886358 |
| Protein Information |
| Protein Name | Superoxide dismutase [Cu-Zn] |
| UniProtKB/SwissProt ID | P0A608 |
| NCBI RefSeq | NP_214946.1 |
| EMBL-CDS | CAB06572.1 |
| UniProtKB Sequence | >sp|P0A608|SODC_MYCTU Superoxide dismutase [Cu-Zn] OS=Mycobacterium tuberculosis GN=sodC PE=1 SV=1
MPKPADHRNHAAVSTSVLSALFLGAGAALLSACSSPQHASTVPGTTPSIWTGSPAPSGLS
GHDEESPGAQSLTSTLTAPDGTKVATAKFEFANGYATVTIATTGVGKLTPGFHGLHIHQV
GKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQVRGDGSAMLVTTTDAFT
MDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
|
| Sequence length | 240 AA |
| Subcellular Location | Associated with cell envelope (or membrane) |
| Function | One of two Mtb superoxide dismutases (SODs) and is a membrane-associated lipoprotein of the Cu, Zn-dependent SOD family. Contributes to the survival of Mtb in activated macrophages, suggesting a role in the defense against the oxidative burst produced in vivo. EC= 1.15.1.1 |
| Protein Structure |
| PDB ID | 1PZS |
| Glycosylation Status |
| Glycosylation Type | O (Ser/Thr) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | T45, T46, S48, T51, S53, S57 |
| Experimentally Validated Glycosite(s ) in Mature Protein | T45, T46, S48, T51, S53, S57 |
| Glycosite(s) Annotated Protein Sequence | >sp|P0A608|SODC_MYCTU Superoxide dismutase [Cu-Zn] OS=Mycobacterium tuberculosis GN=sodC PE=1 SV=1
MPKPADHRNHAAVSTSVLSALFLGAGAALLSACSSPQHASTVPGT*(45)T*(46)PS*(48)IWT*(51)GS*(53)PAPS*(57)GLS
GHDEESPGAQSLTSTLTAPDGTKVATAKFEFANGYATVTIATTGVGKLTPGFHGLHIHQV
GKCEPNSVAPTGGAPGNFLSAGGHYHVPGHTGTPASGDLASLQVRGDGSAMLVTTTDAFT
MDDLLSGAKTAIIIHAGADNFANIPPERYVQVNGTPGPDETTLTTGDAGKRVACGVIGSG
|
| Sequence Around Glycosites (21 AA) | SPQHASTVPGTTPSIWTGSPA
PQHASTVPGTTPSIWTGSPAP
HASTVPGTTPSIWTGSPAPSG
TVPGTTPSIWTGSPAPSGLSG
PGTTPSIWTGSPAPSGLSGHD
PSIWTGSPAPSGLSGHDEESP
|
| Glycosite Sequence Logo | seqlogo |
| Glycosite Sequence Logo |  |
| Technique(s) used for Glycosylation Detection | Concanavalin A (ConA)-binding |
| Technique(s) used for Glycosylated Residue(s) Detection | LC-ESI-MS/MS (liquid chromatography-electrospray-ionization-tandem mass spectrometry) and site-directed mutagenesis (Thr to Ala) |
| Protein Glycosylation- Implication | Glycosylation of this enzyme modulates proteolytic cleavage within the unstructured SodC N-terminus and influences SodC localization and stability. |
| Glycan Information |
| Glycan Annotation | Linkages: αMan-Thr/Ser.
Variable modifications with one to three hexose (mannose) units on each site. The total number of hexose units present is in the range of 6-10. The most dominant SodC glycoform was modified with nine hexose units. |
| Technique(s) used for Glycan Identification | ESI-MS/MS (electrospray ionization tandem mass spctrometry) |
| Protein Glycosylation linked (PGL) gene(s) |
| OST Gene Name | pmt/rv1002c |
| OST NCBI Gene ID | 887882 |
| OST GenBank Gene Sequence | 887882 |
| OST Protein Name | Protein O mannosyltransferase |
| OST UniProtKB/ SwissProt ID | O05586 |
| OST NCBI RefSeq | NP_215518.1 |
| OST EMBL-CDS | CAB08157.1 |
| OST UniProtKB Sequence | >sp|O05586|Y1002_MYCTU Uncharacterized protein Rv1002c/MT1031 OS=Mycobacterium tuberculosis GN=Rv1002c PE=3 SV=2
MVPVVSPGPLVPVADFGPLDRLRGWIVTGLITLLATVTRFLNLGSLTDAGTPIFDEKHYA
PQAWQVLNNHGVEDNPGYGLVVHPPVGKQLIAIGEAIFGYNGFGWRFTGALLGVVLVALV
VRIVRRISRSTLVGAIAGVLLICDGVSFVTARTALLDGFLTFFVVAAFGALIVDRDQVRE
RMHIALLAGRSAATVWGPRVGVRWWRFGAGVLLGLACATKWSGVYFVLFFGAMALAFDVA
ARRQYQVQRPWLGTVRRDVLPSGYALGLIPFAVYLATYAPWFASETAIDRHAVGQAVGRN
SVVPLPDAVRSLWHYTAKAFHFHAGLTNSAGNYHPWESKPWTWPMSLRPVLYAIDQQDVA
GCGAQSCVKAEMLVGTPAMWWLAVPVLAYAGWRMFVRRDWRYAVVLVGYCAGWLPWFADI
DRQMYFFYAATMAPFLVMGISLVLGDILYHPGQGSERRTLGLIVVCCYVALVVTNFAWLY
PVLTGLPISQQTWNLEIWLPSWR
|
| OST EC Number (BRENDA) | 2.4.1.109 |
| OST Genome Context | O05586 |
| Characterized Accessory Gene(s) | Polyprenol-phosphate-mannose (PPM) synthase, Ppm1, is present. A second type of Ppm synthase (Rv3779 gene product) exclusive to slow-growing mycobacteria, is a membrane glycosyltransferase. It mannosylates polyprenyl-phosphates directly from GDP-mannose. |
| PGL Additional Links | CAZy |
| Literatures |
| Reference(s) | 1) Sartain, M.J. and Belisle, J.T. (2009) N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC. Glycobiology, 19, 38-51. [PubMed: 18842962]
2) Scherman, H., Kaur, D., Pham, H., Skovierova, H., Jackson, M. and Brennan, P.J. (2009) Identification of a polyprenylphosphomannosyl synthase involved in the synthesis of mycobacterial mannosides. J Bacteriol, 191, 6769-6772. [PubMed: 19717608]
3) Spagnolo, L., Toro, I., D'Orazio, M., O'Neill, P., |
| Additional Comments | Sec-mediated translocation influences the O-mannosylation. Ppm1 does not discriminate between polyprenol substrates with variable chain lengths and saturation of the isoprene units. |
| Year of Identification | 2000 |
| Year of Validation | 2009 |
