ID Q8ZLI4_SALTY Unreviewed; 797 AA.
AC Q8ZLI4;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=malP {ECO:0000313|EMBL:AAL22376.1};
GN OrderedLocusNames=STM3514 {ECO:0000313|EMBL:AAL22376.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL22376.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL22376.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22376.1; -; Genomic_DNA.
DR RefSeq; NP_462417.1; NC_003197.2.
DR RefSeq; WP_000082246.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLI4; -.
DR STRING; 99287.STM3514; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PaxDb; 99287-STM3514; -.
DR GeneID; 1255037; -.
DR KEGG; stm:STM3514; -.
DR PATRIC; fig|99287.12.peg.3714; -.
DR HOGENOM; CLU_010198_1_1_6; -.
DR OMA; HCACSVA; -.
DR PhylomeDB; Q8ZLI4; -.
DR BioCyc; SENT99287:STM3514-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
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:UP000001014};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 797 AA; 90186 MW; 33B09FDDA9C7EB56 CRC64;
MSQPTFNKDQ FQAALTRQWQ RFGLLSASDM TPRQWWQAVS GALAELLSAQ PVAQPTKGQR
HVNYISMEFL IGRLTGNNLL NLGWYQDVSD VLKAHDINLT DLLEEEVDPA LGNGGLGRLA
ACFLDSMATV GQSATGYGLN YQYGLFRQSF VEGKQMEAPD DWHRGSYPWF RHNEALDVQV
GIGGKVTKEG RWEPGFVITG QAWDLPVLGY RNGVAQPLRL WQATHAHPFD LTKFNDGAFL
RAEQQGIDAE KLTKVLYPND NHTAGKKLRL MQQYFQCACS VADILRRHHL AGRKLHELAD
YEVIQLNDTH PTIAIPELLR VLIDEHQLSW DDAWAITSKT FAYTNHTLMP EALECWDEKL
VKALLPRHMQ IIKQINDRFK TLVDNTWPGD KQVWAKLAVV HDRQVRMANM CVVSGFAVNG
VAALHSDLVV KDLFPEYHQL WPNKFHNVTN GITPRRWIKQ CNPQLAALLD KTLKKEWAND
LDQLINLEKY ADDAKFRQQY RDIKRANKER LVKFIKARTG IEISSNAIFD IQIKRLHEYK
RQHLNLLHIL ALYKEIRENP QADRVPRVFL FGAKAAPGYY LAKNIIFAIN KVAEAINNDP
AVGDKLKVVF LPDYCVSAAE MLIPAADISE QISTAGKEAS GTGNMKLALN GALTVGTLDG
ANVEIAEKVG EENIFIFGHT VEEVKALKAK GYDPVKWRKK DKVLDAVLKE LESGQYSDGD
KHAFDQMLHS LGKQGGDPYL VMADFAAYVE AQKQVDALYR DQEAWTRAAI LNTARCGMFS
SDRSIRDYQA RIWQAKR
//
