ProGP256

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ProGP ID ProGP256
Validation Status Characterized
Organism Information
Organism NameDesulfovibrio gigas
Domain Bacteria
Classification Family: Desulfovibrionaceae
Order: Desulfovibrionales
Class: Deltaproteobacteria or Deltabacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 879
Gene Information
Gene NamehcgA
Protein Information
Protein NameHmcA
UniProtKB Sequence >1Z1N:X|PDBID|CHAIN|SEQUENCE MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAAVFGKLEQPGVVFYHEKHTTALEKMAKDCT SCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEKVVGSYPTAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHG RHVVAEAKRLQVKEDESCKACHHTYDEAQKKLVYAKGEEGSCVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQPDATLLVAGAATANGTVDVNWAAAGPGPVAFDHKAHEGFVGNCV TCHHPTQTGGSLAACGVACHTTTGSKDGNFVTTAQSAHQLGVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQC HEAGFPTSGTQTLGKEEREATAAKILAAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCSGCHHNAKPSLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQEMQVNPKATDCQGCHKPKNSA
Sequence length 560 AA
Subcellular LocationPeriplasm
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 ProteinN290 (N261 position in the crystal structure corresponds to the N290 in full length protein sequence)
Experimentally Validated Glycosite(s ) in Mature ProteinN290
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
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionCrystallographic 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 Identification2007
Year of Identification Month Wise2007.07
Year of Validation 2007
Reference1) Santos-Silva, T., Dias, J.M., Dolla, A., Durand, M.C., Goncalves, L.L., Lampreia, J., Moura, I. and Romao, M.J. (2007) Crystal structure of the 16 heme cytochrome from Desulfovibrio gigas: a glycosylated protein in a sulphate-reducing bacterium. J Mol Biol, 370, 659-673. [PubMed: 17531266]
AuthorSantos-Silva, T., Dias, J.M., Dolla, A., Durand, M.C., Goncalves, L.L., Lampreia, J., Moura, I. and Romao, M.J.
Research GroupREQUIMTE, CQFB, Departamento de Química, FCT-UNL, 2829-516 Caparica, Portugal.
Corresponding Author Romao, M.J.
ContactREQUIMTE, CQFB, Departamento de Química, FCT-UNL, 2829-516 Caparica, Portugal.