ID W1Q2Y3_ABIDE Unreviewed; 807 AA.
AC W1Q2Y3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=GCWU000182_001243 {ECO:0000313|EMBL:ESK65461.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK65461.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK65461.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK65461.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK65461.1}.
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DR EMBL; ACIN03000012; ESK65461.1; -; Genomic_DNA.
DR RefSeq; WP_023391885.1; NZ_KI535340.1.
DR AlphaFoldDB; W1Q2Y3; -.
DR STRING; 592010.GCWU000182_001243; -.
DR GeneID; 84817753; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000019050; Unassembled WGS sequence.
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 NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 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|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000019050};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 644
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 807 AA; 92534 MW; FE4D8E78AB90F87B CRC64;
MKVDAFKDAY KKKFEDMFAV PYTSGSTTEQ FQALGQLLRS IYTDKWVHYN QGKLDSKQKQ
VFYFSMEFLP GRQLKRYLLN LDLLDTARTA LEELGLDFEA VAAAEVDPAL GNGGLGRLAS
CFMDSMAATG VPGNGCGIRY RYGLFKQKFI DGYQIELPEN WLRNPNSWEV RKESKSVIVR
FGGNVWLEAN QYGDLKPVYE NTFDVLAVPY DTPQIGYRND VVNNLRLFTA EIPPGHESYF
TTPEQRKEIQ EITEVLYPDD SNYEGRLLRL KQEYFMCSAG IQSIVRYFKT LDLPWSVFPD
KVAIHINDTH PTLCIPELMR ILVDEESLTW GQAWNIVKKS TSYTNHTILA EAMERWPIYM
IEGLLPRIMQ IIYEINRRHL VNKTALYGAE LAHRTAPIDG DQVLMANLAI IASHSVNGVA
KLHTEILEHY TLRDFKTIYP FRFNNKTNGV THRRWVQLAN EGLSKVLDQH IGNRWRFKPR
EMNILQAFRD NDEVLEQLQE VKLANKERFA RFVKEEMKLD IDPTALFDVQ IKRLHAYKRQ
LLQVMHIVDR YLTLKENPKA DFAKRVFIFG AKAAPSYHYA KSVIKIINEL ANLVNNDPAI
GDKIKIVFVE NYGVSLAELI IPAANLSEQI SLAGKEASGT SNMKLMANGA LTMATLDGAN
VEIYDLVGDD NIFLFGMTAD DVQKLREANN YYSRAIYEEN PQIKRVLNAF IDGTIPNIEA
EGREIFDSLV LYNDEYFLLQ DYPSFYEAQM AADKLYQEPK EWAKRALTNI AYSGKFSSDY
TILRYAESIW NVSPETNLLG EGFSNLD
//
