Reviewed, UniProtKB/Swiss-Prot P39123 (PHSG_BACSU)

Names and origin

Protein names

Recommended name:
    Glycogen phosphorylase
    EC=2.4.1.1

Gene names

Name:	glgP
Ordered Locus Names:	BSU30940

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor	Pyridoxal phosphate.
Induction	Expressed exclusively on media containing carbon sources that allow efficient sporulation.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	glycogen 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
Molecule processing
	Chain	1 – 798	798	Glycogen phosphorylase		PRO_0000188549
Amino acid modifications
	Modified residue	646	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39123-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 2E5FD08F05C75045	FASTA	798	91,756
	10 20 30 40 50 60 MFSSKERFAD LFLKRLEMTC GKSFKDSAKL DQYKTLGNMV REYISADWIE TNEKSRSNSG 70 80 90 100 110 120 KQTYYLSIEF LLGQLLEQNL MNLGVRDVVE AGLKEIGINL EEILQIENDA GLGNGGLGRL 130 140 150 160 170 180 AACFLDSLAS LNLPGHGMGI RYKHGLFEQK IVDGHQVELP EQWLKNGNVW EVRNADQAVD 190 200 210 220 230 240 VPFWGEVHMT EKSGRLHFRH EQATIVTAVP YDIPIIGYET GTVNTLRLWN AEPYAHYHGG 250 260 270 280 290 300 NILSYKRETE AVSEFLYPDD THDEGKILRL KQQYFLVCAS LKSIVNNYRK THKSLSGLHK 310 320 330 340 350 360 KVSIHINDTH PALAVPELMR ILLDEENMSW EEAWHITVHT ISYTNHTTLS EALEKWPIHL 370 380 390 400 410 420 FKPLLPRMYM IIEEINERFC RAVWEKYPGD WKRIENMAIT AHGVVKMAHL AIVGSYSVNG 430 440 450 460 470 480 VAKIHSDILK EREMRDFHLL FPNRFNNKTN GIAHRRWLLK ANPGLSAIIT EAIGDEWVKQ 490 500 510 520 530 540 PESLIRLEPY ATDPAFIEQF QNNKSKKKQE LADLIFCTAG VVVNPESIFD VQVKRLHAYK 550 560 570 580 590 600 RQLLNVLHIM YLYNRLKEDS GFSIYPQTFI FGAKASPSYY YAKKIIKLIH SVAEKVNYDP 610 620 630 640 650 660 AVKQLIKVVF LENYRVSMAE RIFPASDVSE QISTASKEAS GTGNMKFMMN GALTIGTHDG 670 680 690 700 710 720 ANIEILERVG PDCIYTFGLK ADEVLSYQEN GGYRSREYYQ HDRRIRQVAD QLINGFFEGE 730 740 750 760 770 780 ADEFESIFDS LLPHNDEYFV LKDFSSYADA QERIQADYRE RRKWSEHSIV NIAHSGYFSS 790 DRTIREYAKD IWGIKPMM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glycogen in Bacillus subtilis: molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation." Kiel J.A.K.W., Boels J.M., Beldman G., Venema G. Mol. Microbiol. 11:203-218(1994) [PubMed: 8145641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z25795 Genomic DNA. Translation: CAA81044.1. AF008220 Genomic DNA. Translation: AAC00218.1. AL009126 Genomic DNA. Translation: CAB15072.1.
PIR	S40052.
RefSeq	NP_390972.1.
3D structure databases
HSSP	HSSP built from PDB template 1YGP based on UniProtKB P06738.
ModBase	Search...
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
PTM databases
PhosSite	P39123.
Genome annotation databases
GeneID	936630.
GenomeReviews	Gene locus BSU30940 in contig AL009126_GR.
KEGG	bsu:BSU30940.
NMPDR	fig|224308.1.peg.3097.
Organism-specific databases
SubtiList	BG10911. glgP. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P39123.
OMA	LWKAEAT.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3089-MON.
BRENDA	2.4.1.1. 150.
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

PHSG_BACSU

Accession

Primary (citable) accession number: P39123

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)