ProGlyProt IDBC138
Organism Information
Organism NameDesulfovibrio gigas
DomainBacteria
ClassificationFamily: Desulfovibrionaceae
Order: Desulfovibrionales
Class: Deltaproteobacteria or Deltabacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)879
Genome Sequence (s)
EMBL
Gene Information
Gene NamehcgA
NCBI Gene ID
Protein Information
Protein NameHmcA
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence>1Z1N:X|PDBID|CHAIN|SEQUENCE MTQRKRAARWVGIPCAILFLTVPFISATASTPGPASTAEPKVDAIVIDTAAVFGKLEQPGVVFYHEKHTTALEKMAKDCT SCHVETEGKLSFKFARTVDPTSKNAMAEQYHANCMACHEKVVGSYPTAPQAAECKRCHVGPGVEGATVTPKPSLDLNLHG RHVVAEAKRLQVKEDESCKACHHTYDEAQKKLVYAKGEEGSCVYCHKQEPLPSPVQQDRVVPSTRDASHESCVNCHLSTR KAQTESGPVLCVGCHTAEAQAAWKKTAETPRLFRGQPDATLLVAGAATANGTVDVNWAAAGPGPVAFDHKAHEGFVGNCV TCHHPTQTGGSLAACGVACHTTTGSKDGNFVTTAQSAHQLGVTTSCVGCHTTQANARKECAGCHAPMQKTALSQNSCIQC HEAGFPTSGTQTLGKEEREATAAKILAAKDEKPKTVPLENVPEKLTLNYMDEKGDEWQAAEFPHRKIYQKLVEEAAKSPM ANHFHGDALTMCSGCHHNAKPSLNPPKCASCHSKPFQERTANQPGLKGAFHNQCIGCHQEMQVNPKATDCQGCHKPKNSA
Sequence length560 AA
Subcellular LocationPeriplasm
FunctionA 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 ID1Z1N
Glycosylation Status
Glycosylation TypeN (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 Logoseqlogo
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) DetectionCrystallographic analysis (electron density maps)
Protein Glycosylation- ImplicationCarbohydrate 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 AnnotationTrisaccharide (NAG,NAA,any epimer of NAG); AllNacGlcNAc-Asn linkage; NAA is (epimer of NAG) N-acetylallosamine.
Technique(s) used for Glycan IdentificationCrystallographic analysis (electron density maps)
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
OST NCBI Gene ID
OST GenBank Gene Sequence
OST Protein Name
OST UniProtKB/ SwissProt ID
OST NCBI RefSeq
OST EMBL-CDS
OST UniProtKB Sequence
OST EC Number (BRENDA)
OST Genome Context
Characterized Accessory Gene(s)
PGL Additional LinksCAZy
Literatures
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]
Additional Comments
Year of Identification2007
Year of Validation2007