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ProGlyProt ID
BC138
Organism Information
Organism Name
Desulfovibrio gigas
Domain
Bacteria
Classification
Family: Desulfovibrionaceae
Order: Desulfovibrionales
Class: Deltaproteobacteria or Deltabacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
 
 
Gene Information
Gene Name
hcgA
 
 
Protein Information
Protein Name
HmcA
UniProtKB Sequence
>1Z1N:X|PDBID|CHAIN|SEQUENCE MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAA
VFGKLEQPGVVFYHEKHTTALEKMAKDCT SCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEKVVGSYP
TAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHG RHVVAEAKRLQVKEDESCKACHHTYDEAQKKLVYAKGEEGS
CVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQ
PDATLLVAGAATANGTVDVNWAAAGPGPVAFDHKAHEGFVGNCV TCHHPTQTGGSLAACGVACHTTTGSKDGNFV
TTAQSAHQLGVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQC HEAGFPTSGTQTLGKEEREATAAKIL
AAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCSGCHHNAKP
SLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQEMQVNPKATDCQGCHKPKNSA
Sequence length
560 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
 
 
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 MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAA
VFGKLEQPGVVFYHEKHTTALEKMAKDCT SCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEKVVGSYP
TAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHG RHVVAEAKRLQVKEDESCKACHHTYDEAQKKLVYAKGEEGS
CVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQ
PDATLLVAGAATAN*(290)GTVDVNWAAAGPGPVAFDHKAHEGFVGNCV TCHHPTQTGGSLAACGVACHTTT
GSKDGNFVTTAQSAHQLGVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQC HEAGFPTSGTQTLGKEER
EATAAKILAAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCS
GCHHNAKPSLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQEMQVNPKATDCQGCHKPKNSA
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
Reference(s)
1) 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]
Year of Identification
2007
Year of Validation
2007
 
 
Copyright @ 2011 IMTECH
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