Q51225 (Q51225_NEIME) Unreviewed, UniProtKB/TrEMBL

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. SAAS SAAS003016

Ontologies

Keywords
Domain	Lipoyl 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 nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
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)
	Q51225 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 24823E854A29CA62	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

References

[1]	"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: 10234839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: B:4:P1.15 EMBL CAA54878.1.
[2]	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.
[3]	"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: 9193005] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD.
[4]	"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: 10089406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.18 ANGSTROMS) OF 112-593 IN COMPLEX WITH FAD.
+	Additional computationally mapped references.

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

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]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

PANTHER

PTHR22912:SF20. Lipoamide_DH. 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...

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:	July 27, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)