ID A0A0H3GYH4_KLEPH Unreviewed; 796 AA.
AC A0A0H3GYH4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=KPHS_49390 {ECO:0000313|EMBL:AEW63637.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW63637.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW63637.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW63637.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
RN [2] {ECO:0007829|PDB:7TM7}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP 5'-PHOSPHATE.
RA Liu L., Lovell S., Battaile K.P., Tillery L., Shek R., Craig J.K.,
RA Barrett L.K., Van Voorhis W.C.;
RT "Crystal structure of Alpha-1,4 glucan phosphorylase from Klebsiella
RT pneumoniae.";
RL Submitted (JAN-2022) to the PDB data bank.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001275,
CC ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP003200; AEW63637.1; -; Genomic_DNA.
DR RefSeq; WP_004151407.1; NC_016845.1.
DR RefSeq; YP_005229239.1; NC_016845.1.
DR PDB; 7TM7; X-ray; 1.91 A; A/B=1-796.
DR AlphaFoldDB; A0A0H3GYH4; -.
DR SMR; A0A0H3GYH4; -.
DR STRING; 1125630.KPHS_49390; -.
DR GeneID; 11850008; -.
DR KEGG; kpm:KPHS_49390; -.
DR PATRIC; fig|1125630.4.peg.4825; -.
DR HOGENOM; CLU_010198_1_1_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF25; MALTODEXTRIN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7TM7};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT BINDING 534
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0007829|PDB:7TM7"
FT BINDING 642
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0007829|PDB:7TM7"
FT BINDING 643
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0007829|PDB:7TM7"
FT BINDING 646
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="covalent"
FT /evidence="ECO:0007829|PDB:7TM7"
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 796 AA; 90059 MW; BCE208F1613D5155 CRC64;
MSQTTFNKAQ FQAALTRQWQ HFGLQSASEM TQRQWWRAVS GALAELLAAQ PVAKPAQGQR
HVNYISMEFL IGRLTGNNLL NLGWYEGVSD ALKGYDVNLT DLLEEETDPA LGNGGLGRLA
ACFLDSMATV GQSATGYGLN YQYGLFRQSF DDGQQMEAPD DWGRSSYPWF RHNEALDVQV
GIGGKVSKNG EWQPAFVITG EAWDLPVLGY RNNVAQPLRL WQAKHAHPFN LTKFNDGDFL
RAEQQGIDAE KLTKVLYPND NHQAGKKLRL MQQYFQCACS VADILRRHHL AGRKLAELAD
YEVIQLNDTH PTIAIPELLR VLIDEHQLSW DDAWAITSKT FAYTNHTLMP EALECWDEKL
VKALLPRHMQ IIKEINDRFK QLVDKTWPGD KQVWAKLAVV HDKQVRMANM CVVGGFAVNG
VAALHSDLVV KDLFPEYNQL WPNKFHNVTN GITPRRWIKQ CNPALASLLD ETLKKEWAND
LDQLINLEKY ADDAAFRQTY RDIKQANKVH LAEFVKQRTG IEINPQAIFD IQIKRLHEYK
RQHLNLLHIL ALYKEIRENP QSDRVPRVFL FGAKAAPGYY LAKNIIFAIN KVAEAINNDP
KVGDKLKVVF LPDYCVSAAE KLIPAADISE QISTAGKEAS GTGNMKLALN GALTVGTLDG
ANVEIAEQVG EENIFIFGHT VEEVKALKAK GYDPLKWRKK DKLLDAVLKE LENGTYSNGD
KHAFDQMLHS LLQGGDPYLV LADFEAYVAA QKRVDELYRD EEAWTRAAIL NTARCGMFSS
DRSIRDYQQR IWQAKR
//
