Q8KQ56 (Q8KQ56_9CORY) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: Phosphorylase RuleBase RU000587 EC=2.4.1.1 RuleBase RU000587
Organism	Corynebacterium callunae EMBL AAM52219.1
Taxonomic identifier	1721 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties By similarity. RuleBase RU000587
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. RuleBase RU000587
Cofactor	Pyridoxal phosphate By similarity. RuleBase RU000587
Sequence similarities	Belongs to the glycogen phosphorylase family. RuleBase RU004179

Ontologies

Keywords
Biological process	Carbohydrate metabolism RuleBase RU000587
Ligand	Pyridoxal phosphate PDB 2C4M
Molecular function	Glycosyltransferase RuleBase RU000587 EMBL AAM52219.1 Transferase
Technical term	3D-structure PDB 2C4M
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphorylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	635	1	Pyridoxal phosphate PDB 2C4M

Sequences

	Sequence		Length	Mass (Da)
	Q8KQ56 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D4A7B2967C42D75D	FASTA	796	90,576
	10 20 30 40 50 60 MSPEKQPLPA ALVGSHVRAA AGTPADLATD RKFWTGLSRA VQERIADDWE RTREAYGAAR 70 80 90 100 110 120 QQHYFSAEFL MGRALLNNLT NLGLVDEAAA ATRELGHELT DILEIENDAA LGNGGLGRLA 130 140 150 160 170 180 ACFLDSAVTQ DYPVTGYGLL YRFGLFRQSF NEGFQVEKPD PWREEEYPFT IRRASDQLVV 190 200 210 220 230 240 CFDDMKTRAI PYDMPITGYG THNVGTLRLW KAEPWEEFDY DAFNSQRFTD AIIERERVSD 250 260 270 280 290 300 ICRVLYPNDT TYEGKKLRVR QQYFFTSASL QAMIQDHLAH HKDLSNFAEF HSVQLNDTHP 310 320 330 340 350 360 VLAIPELMRL LMDEHDMGWE ESWAIVSKTF AYTNHTVLTE ALEQWDEQIF QQLFWRVWEI 370 380 390 400 410 420 IAEIDRRFRL ERAADGLDEE TINRMAPIQH GTVHMAWIAC YAAYSINGVA ALHTEIIKAE 430 440 450 460 470 480 TLADWYALWP EKFNNKTNGV TPRRWLRMIN PGLSDLLTRL SGSDDWVTDL DELKKLRSYA 490 500 510 520 530 540 DDKSVLEELR AIKAANKQDF AEWILERQGI EIDPESIFDV QIKRLHEYKR QLMNALYVLD 550 560 570 580 590 600 LYFRIKEDGL TDIPARTVIF GAKAAPGYVR AKAIIKLINS IADLVNNDPE VSPLLKVVFV 610 620 630 640 650 660 ENYNVSPAEH ILPASDVSEQ ISTAGKEASG TSNMKFMMNG ALTLGTMDGA NVEIVDSVGE 670 680 690 700 710 720 ENAYIFGARV EELPALRESY KPYELYETVP GLKRALDALD NGTLNDNNSG LFYDLKHSLI 730 740 750 760 770 780 HGYGKDASDT YYVLGDFADY RETRDRMAAD YASDPLGWAR MAWINICESG RFSSDRTIRD 790 YATEIWKLEP TPAVKK

References

[1]	"Quarternary interactions in dimeric starch phosphorylase from Corynebacterium callunae and their dependence on phosphate." Griessler R., Mucha J., Nidetzky B. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Starch Phosphorylase: Structural Studies Explain Oxyanion-Dependent Kinetic Stability and Regulatory Control." Purvis A., Nidetzky B., Watson K. Submitted (OCT-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-635.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY102616 Genomic DNA. Translation: AAM52219.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C4M	X-ray	1.90	A/B/C/D	1-796	[»]

ProteinModelPortal

Q8KQ56.

SMR

Q8KQ56. Positions 6-795.

ModBase

Search...

Protein family/group databases

CAZy

GT35. Glycosyltransferase Family 35.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]

PANTHER

PTHR11468. Glyco_trans_35. 1 hit.

Pfam

PF00343. Phosphorylase. 1 hit.
[Graphical view]

PIRSF

PIRSF000460. Pprylas_GlgP. 1 hit.

TIGRFAMs

TIGR02093. P_ylase. 1 hit.

PROSITE

PS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q8KQ56_9CORY

Accession

Primary (citable) accession number: Q8KQ56

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2002
Last sequence update:	October 1, 2002
Last modified:	April 5, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)