Outer membrane protein p64k or PM-6 - Neisseria meningitidis

Preferred order of sections

Names and origin

Protein names

Submitted name:
Outer membrane protein p64k or PM-6 EMBL CAA54878.1

Gene names

Name:

m-6 EMBL CAA54878.1

Organism

Neisseria meningitidis EMBL CAA54878.1

Taxonomic identifier

487 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Cofactor	Binds 1 lipoyl cofactor covalently By similarity. SAAS SAAS003016
Sequence similarities	Contains 1 lipoyl-binding domain. RuleBase RU000447 SAAS SAAS003016

Ontologies

Keywords
Domain	Lipoyl RuleBase RU000447 SAAS SAAS003016
Ligand	FAD PDB 1BHY PDB 1OJT Flavoprotein PDB 1BHY PDB 1OJT Nucleotide-binding PDB 1BHY PDB 1OJT
Technical term	3D-structure PDB 1BHY PDB 1OJT
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

127 – 128

2

FAD PDB 1BHY PDB 1OJT

Nucleotide binding

147 – 148

2

FAD PDB 1BHY PDB 1OJT

Nucleotide binding

160 – 161

2

FAD PDB 1BHY PDB 1OJT

Nucleotide binding

227 – 228

2

FAD PDB 1BHY PDB 1OJT

Sites

Binding site

155

1

FAD; via amide nitrogen PDB 1BHY PDB 1OJT

Binding site

165

1

FAD PDB 1BHY PDB 1OJT

Binding site

246

1

FAD PDB 1BHY PDB 1OJT

Binding site

435

1

FAD PDB 1BHY PDB 1OJT

Binding site

443

1

FAD; via amide nitrogen PDB 1BHY PDB 1OJT

Binding site

567

1

FAD; via carbonyl oxygen PDB 1BHY PDB 1OJT

Sequences

Sequence

Length

Mass (Da)

Tools

Q51225 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 24823E854A29CA62
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FASTA

594

61,883

        10         20         30         40         50         60 
MALVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA EVAGVVKEVK 

        70         80         90        100        110        120 
VKVGDKISEG GLIVVVEAEG TAAAPKAEAA AAPAQEAPKA AAPAPQAAQF GGSADAEYDV 

       130        140        150        160        170        180 
VVLGGGPGGY SAAFAAADEG LKVAIVERYK TLGGVCLNVG CIPSKALLHN AAVIDEVRHL 

       190        200        210        220        230        240 
AANGIKYPEP ELDIDMLRAY KDGVVSRLTG GLAGMAKSRK VDVIQGDGQF LDPHHLEVSL 

       250        260        270        280        290        300 
TAGDAYEQAA PTGEKKIVAF KNCIIAAGSR VTKLPFIPED PRIIDSSGAL ALKEVPGKLL 

       310        320        330        340        350        360 
IIGGGIIGLE MGTVYSTLGS RLDVVEMMDG LMQGADRDLV KVWQKQNEYR FDNIMVNTKT 

       370        380        390        400        410        420 
VAVEPKEDGV YVTFEGANAP KEPQRYDAVL VAAGRAPNGK LISAEKAGVA VTDRGFIEVD 

       430        440        450        460        470        480 
KQMRTNVPHI YAIGDIVGQP MLAHKAVHEG HVAAENCAGH KAYFDARVIP GVAYTSPEVA 

       490        500        510        520        530        540 
WVGETELSAK ASGRKITKAN FPWAASGRAI ANGCDKPFTK LIFDAETGRI IGGGIVGPNG 

       550        560        570        580        590 
GDMIGEVCLA IEMGCDAADI GKTIHPHPTL GESIGMAAEV ALGTCTDLPP QKKK

« Hide

References

[1]	Guillen G.G.G.N. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: B:4:P1.15 EMBL CAA54878.1.
[2]	"Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis." Li de la Sierra I., Pernot L., Prange T., Saludjian P., Schiltz M., Fourme R., Padron G. J. Mol. Biol. 269:129-141(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD.
[3]	"Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values." Ramin M., Shepard W., Fourme R., Kahn R. Acta Crystallogr. D 55:157-167(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.18 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD.
[4]	"Characterisation of the lpdA gene from Neisseria meningitidis by polymerase chain reaction, restriction fragment length polymorphism and sequencing." Silva R., Menendez T., Alonso L.M., Iglesias E., Musacchio A., de Jesus Leal M., Alvarez A., Couizeau E., Martin A., Herrera L.S., Guillen G. FEMS Microbiol. Lett. 174:191-199(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: B:4:P1.15 EMBL CAA54878.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X77920 Genomic DNA. Translation: CAA54878.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BHY	X-ray	4.18	A	112-593	[»]
1OJT	X-ray	2.75	A	112-593	[»]

ProteinModelPortal

Q51225.

SMR

Q51225. Positions 2-82, 112-593.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR011053. Single_hybrid_motif.
[Graphical view]

PANTHER

PTHR22912:SF20. PTHR22912:SF20. 1 hit.

Pfam

PF00364. Biotin_lipoyl. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
SSF51230. Hybrid_motif. 1 hit.

TIGRFAMs

TIGR01350. lipoamide_DH. 1 hit.

PROSITE

PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q51225.

Entry information

Entry name

Q51225_NEIME

Accession

Primary (citable) accession number: Q51225

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)