ID Q30JZ8_VIBCL Unreviewed; 273 AA.
AC Q30JZ8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Flags: Fragment;
GN Name=malP {ECO:0000313|EMBL:AAY87642.1};
OS Vibrio cholerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666 {ECO:0000313|EMBL:AAY87642.1};
RN [1] {ECO:0000313|EMBL:AAY87642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=#75 {ECO:0000313|EMBL:AAY87651.1}, 395
RC {ECO:0000313|EMBL:AAY87636.1}, and 905-93
RC {ECO:0000313|EMBL:AAY87642.1};
RX PubMed=16318732;
RA Salim A., Lan R., Reeves P.R.;
RT "Vibrio cholerae pathogenic clones.";
RL Emerg. Infect. Dis. 11:1758-1760(2005).
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 -!- 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|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={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; DQ021143; AAY87636.1; -; Genomic_DNA.
DR EMBL; DQ021149; AAY87642.1; -; Genomic_DNA.
DR EMBL; DQ021158; AAY87651.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30JZ8; -.
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:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR000811; Glyco_trans_35.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF25; MALTODEXTRIN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY87642.1"
FT NON_TER 273
FT /evidence="ECO:0000313|EMBL:AAY87642.1"
SQ SEQUENCE 273 AA; 30946 MW; 323F4609812957D9 CRC64;
LLETEQDERI LNSKSLNYLS LEFLIGRLTG NNLISMGVYE AVAEAMEELG QNLSDLLEEE
RDPSLGNGGL GRLAACFMDS CAAQEYPTVG YGLHYEYGLF KQSFEEGRQK EAPDAWCGVE
GYPWEVARPE LKQEIGFYGH VEVVNENGKE RRRWVPGMLV QAMPWDLPIV GYQSDTVYPL
RLWECRAIAP FSLESFNNGN YFEAQHALID AGNITKVLYP NDNHEKGKTL RLMQQYFHSA
ASVRDILRRH EAAGHALADL PKYETIQLND THP
//
