ProGP255 (HmcA)
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| ProGP ID | ProGP255 (HmcA) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Desulfovibrio gigas |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Deltaproteobacteria Orders : Desulfovibrionales Family : Desulfovibrionaceae Genus : Desulfovibrio Species : gigas |
| Taxonomic ID (NCBI) | 879 |
| Genome Information | |
| GenBank | AJ318781 |
| EMBL | AJ318781 |
| Gene Information | |
| Gene Name | hcgA |
| GenBank Gene Sequence | CP006585.1 |
| Protein Information | |
| Protein Name | HmcA |
| UniProtKB/SwissProt ID | T2G9Q2 |
| NCBI RefSeq | AGW12617.1 |
| EMBL-CDS | AGW12617.1 |
| UniProtKB Sequence | >tr|T2G9Q2|T2G9Q2_DESGI Sixteen Heme Cytochrome OS=Desulfovibrio gigas DSM 1382 = ATCC 19364 GN=hmcA PE=1 SV=1 MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAAVFGKLEQPG VVFYHEKHTTALEKMAKDCTSCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEK VVGSYPTAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHGRHVVAEAKRLQVKEDESCKA CHHTYDEAQKKLVYAKGEEGSCVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQPDATLLVAGAATANGTVDVNWAAA GPGPVAFDHKAHEGFVGNCVTCHHPTQTGGSLAACGVACHTTTGSKDGNFVTTAQSAHQL GVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQCHEAGFPTSGTQTLGKEEREA TAAKILAAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCSGCHHNAKPSLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQE MQVNPKATDCQGCHKPKNS |
| Sequence length | 559 AA |
| Subcellular Location | Periplasm |
| Function | A high molecular mass cytochrome that harbours 16 c-type heme groups. Involved in electron transfer from the periplasm to the cytoplasm. The high molecular mass complex Hmc (HmcA & HmcF) from Desulfovibrio sp. has been proposed to be involved in the bridge between periplasmic hydrogen oxidation and cytoplasmic sulphate reduction in Desulfovibrio gigas. |
| Protein Structure | |
| PDB ID | 1Z1N |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N290 (N261 position in the crystal structure corresponds to the N290 in full length protein sequence) |
| Experimentally Validated Glycosite(s ) in Mature Protein | N290 |
| Glycosite(s) Annotated Protein Sequence | >1Z1N:X|PDBID|CHAIN|SEQUENCE MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAAVFGKLEQPGVVFYHEKHTTALEKMAKDCT SCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEKVVGSYPTAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHG RHVVAEAKRLQVKEDESCKACHHTYDEAQKKLVYAKGEEGSCVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQPDATLLVAGAATAN*(290)GTVDVNWAAAGPGPVAFDHKAHEGFVGNCV TCHHPTQTGGSLAACGVACHTTTGSKDGNFVTTAQSAHQLGVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQC HEAGFPTSGTQTLGKEEREATAAKILAAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCSGCHHNAKPSLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQEMQVNPKATDCQGCHKPKNSA |
| Sequence Around Glycosites (21 AA) | TLLVAGAATANGTVDVNWAAA |
| Technique(s) used for Glycosylation Detection | Crystallographic analysis (electron density maps), GlycoProfile III carbohydrate detection kit (using periodic acid as oxidizing agent), MALDI-TOF(matrix-assisted laser desorption/ionization time-of-flight) |
| Technique(s) used for Glycosylated Residue(s) Detection | Crystallographic analysis (electron density maps) |
| Protein Glycosylation- Implication | Carbohydrate could be acting as an anchor of the protein to the phospholipidic membrane. The carbohydrate bound to HmcA may also contribute to the maintenance of the protein conformation and stability as well as to a protection mechanism against proteases. |
| Glycan Information | |
| Glycan Annotation | Trisaccharide (NAG,NAA,any epimer of NAG); AllNacGlcNAc-Asn linkage; NAA is (epimer of NAG) N-acetylallosamine. |
| Technique(s) used for Glycan Identification | Crystallographic analysis (electron density maps) |
| Literature | |
| Year of Identification | 2007 |
| Year of Identification Month Wise | 2007.07 |
| Year of Validation | 2007 |
| Reference | Santos-Silva, T., Dias, J.M., Dolla, A., Durand, M.C., Gonçalves, L.L., Lampreia, J., Moura, I. and Romão, M.J., 2007. Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: a glycosylated protein in a sulphate-reducing bacterium. Journal of molecular biology, 370(4), pp.659-673. |
| Corresponding Author | Maria João Romão |
| Contact | REQUIMTE, CQFB, Departamento de Química, FCT-UNL, 2829-516 Caparica, Portugal. |