Q945K2 (Q945K2_PRUDU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
R-oxynitrile lyase isoenzyme 1 EMBL AAL11514.1

Gene names

Name:

hnl1 EMBL AAL11514.1

Organism

Prunus dulcis (Almond) (Prunus amygdalus) EMBL AAL11514.1

Taxonomic identifier

3755 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Maloideae › Amygdaleae › Prunus

Protein attributes

Sequence length	563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Cofactor	FAD By similarity. RuleBase RU003968
Sequence similarities	Belongs to the GMC oxidoreductase family. RuleBase RU003968

Ontologies

Keywords
Domain	Signal EMBL AAL11514.1
Ligand	FAD PDB 1JU2 PDB 3GDN PDB 3GDP Flavoprotein RuleBase RU003968 PDB 1JU2 PDB 3GDN PDB 3GDP Nucleotide-binding PDB 1JU2 PDB 3GDN PDB 3GDP
Molecular function	Lyase EMBL AAL11514.1
Technical term	3D-structure PDB 1JU2 PDB 3GDN PDB 3GDP
Gene Ontology (GO)
Biological process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	choline dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro lyase activity Inferred from electronic annotation. Source: UniProtKB-KW 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
Molecule processing
	Signal peptide	1 – 27	27	Potential EMBL AAL11514.1
	Chain	28 – 563	536	Potential EMBL AAL11514.1		PRO_5000061321
Regions
	Nucleotide binding	63 – 64	2	FAD PDB 1JU2 PDB 3GDN PDB 3GDP
	Nucleotide binding	82 – 83	2	FAD PDB 1JU2 PDB 3GDN PDB 3GDP
	Nucleotide binding	137 – 140	4	FAD PDB 1JU2 PDB 3GDN PDB 3GDP
	Nucleotide binding	485 – 486	2	FAD PDB 3GDN PDB 3GDP
	Nucleotide binding	525 – 526	2	FAD PDB 1JU2 PDB 3GDN PDB 3GDP
Sites
	Binding site	129	1	FAD; via carbonyl oxygen PDB 1JU2 PDB 3GDN PDB 3GDP
	Binding site	133	1	FAD PDB 1JU2 PDB 3GDN PDB 3GDP
	Binding site	198	1	Mannose PDB 1JU2 PDB 3GDP
	Binding site	244	1	FAD; via amide nitrogen and carbonyl oxygen PDB 1JU2 PDB 3GDN PDB 3GDP
	Binding site	514	1	FAD; via amide nitrogen PDB 1JU2 PDB 3GDN PDB 3GDP
Amino acid modifications
	Glycosylation	145	1	N-linked (GlcNAc...) PDB 1JU2 PDB 3GDN PDB 3GDP
	Glycosylation	162	1	N-linked (GlcNAc...) PDB 1JU2 PDB 3GDN PDB 3GDP
	Glycosylation	379	1	N-linked (GlcNAc...) PDB 1JU2 PDB 3GDP
	Glycosylation	419	1	N-linked (GlcNAc...) PDB 1JU2 PDB 3GDN PDB 3GDP

Sequences

	Sequence		Length	Mass (Da)
	Q945K2 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E0F53C236F4B001C	FASTA	563	61,158
	10 20 30 40 50 60 MEKSTMSAIL LVLYIFVLHL QYSEVHSLAT TSDHDFSYLS FAYDATDLEL EGSYDYVIVG 70 80 90 100 110 120 GGTSGCPLAA TLSEKYKVLV LERGSLPTAY PNVLTADGFV YNLQQEDDGK TPVERFVSED 130 140 150 160 170 180 GIDNVRGRVL GGTSIINAGV YARANTSIYS ASGVDWDMDL VNQTYEWVED TIVYKPNSQS 190 200 210 220 230 240 WQSVTKTAFL EAGVHPNHGF SLDHEEGTRI TGSTFDNKGT RHAADELLNK GNSNNLRVGV 250 260 270 280 290 300 HASVEKIIFS NAPGLTATGV IYRDSNGTPH QAFVRSKGEV IVSAGTIGTP QLLLLSGVGP 310 320 330 340 350 360 ESYLSSLNIP VVLSHPYVGQ FLHDNPRNFI NILPPNPIEP TIVTVLGISN DFYQCSFSSL 370 380 390 400 410 420 PFTTPPFGFF PSASYPLPNS TFAHFASKVA GPLSYGSLTL KSSSNVRVSP NVKFNYYSNL 430 440 450 460 470 480 TDLSHCVSGM KKIGELLSTD ALKPYKVEDL PGVEGFNILG IPLPKDQTDD AAFETFCRES 490 500 510 520 530 540 VASYWHYHGG CLVGKVLDGD FRVTGINALR VVDGSTFPYT PASHPQGFYL MLGRYVGIKI 550 560 LQERSASDLK ILDSLKSAAS LVL

References

[1]	"The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase." Dreveny I., Gruber K., Glieder A., Thompson A., Kratky C. Structure 9:803-815(2001) [PubMed: 11566130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Seed EMBL AAL11514.1.
[2]	Glieder A.S., Dreveny I., Mandl H., Majer S., Schwab H. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Seed EMBL AAL11514.1.
[3]	"Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity." Dreveny I., Andryushkova A.S., Glieder A., Gruber K., Kratky C. Biochemistry 48:3370-3377(2009) [PubMed: 19256550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 28-548 IN COMPLEX WITH FAD AND MANNOSE, GLYCOSYLATION AT ASN-145; ASN-162; ASN-379 AND ASN-419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF412329 Genomic DNA. Translation: AAL11514.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JU2	X-ray	1.47	A/B	28-563	[»]
3GDN	X-ray	1.67	A/B	28-548	[»]
3GDP	X-ray	1.57	A/B	28-548	[»]

ProteinModelPortal

Q945K2.

SMR

Q945K2. Positions 28-548.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Enzyme and pathway databases

BRENDA

4.1.2.10. 1961.

Family and domain databases

InterPro

IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]

Pfam

PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000137. Alcohol_oxidase. 1 hit.

PROSITE

PS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q945K2_PRUDU

Accession

Primary (citable) accession number: Q945K2

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	October 19, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)