ID A5Z676_9FIRM Unreviewed; 826 AA.
AC A5Z676;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:EDM51643.1};
GN ORFNames=EUBVEN_01209 {ECO:0000313|EMBL:EDM51643.1};
OS Eubacterium ventriosum ATCC 27560.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM51643.1, ECO:0000313|Proteomes:UP000006000};
RN [1] {ECO:0000313|EMBL:EDM51643.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM51643.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM51643.1, ECO:0000313|Proteomes:UP000006000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM51643.1,
RC ECO:0000313|Proteomes:UP000006000};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560).";
RL Submitted (APR-2007) 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 -!- 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}.
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:EDM51643.1}.
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DR EMBL; AAVL02000032; EDM51643.1; -; Genomic_DNA.
DR AlphaFoldDB; A5Z676; -.
DR STRING; 411463.EUBVEN_01209; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000006000; 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 InterPro; IPR035090; Pyridoxal_P_attach_site.
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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 663
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 826 AA; 95335 MW; 5DBAC25CF13A528C CRC64;
MAKNEGMEKH EEFKAEFKKR VKEQAKMLYR KSLDEISDRH KFVCVAYAVK DIVIDQWIAT
QKAYDEKDAK IVYYLSMEFL MGRALGNMII NLSSRDEIKE AIEELGLDLN VIEDQEPDAA
LGNGGLGRLA ACFLDSLSTL NYPAYGCGIR YKYGMFQQKI ENGYQKEIPE DWLRHANPLE
IKREEYACEV KFGGYVRVEN RDGRNYFIQE GYQSVNAIPY DMPIVGYGNN VVNTLRIWDA
EPVVHFNLDE FDKGSYMAAV EQENLAKTIT EVLYPNDNHY AGKELRLKQQ YFFVSASLQT
AIKKYLKNHD DIRKLPEKVV FQMNDTHPTL TVAELMRLLM DEYNLEWDEA WDITTHACAY
TNHTIMSEAL EKWPIELFSR LLPRCYQIIE EINRRFCIEI ENKYPGNHDK VAKMAIIYDG
QVKMAHLAIC AGFSVNGVAK LHTEILKHQE LKDFYEMMPE KFNNKTNGIT QRRFLLHANP
LLSEWVTGKV GDDWITDLPK IKGIEVYADD KKAQAEFMNI KYQNKVRLAK YIKEHNGIDV
DPRSIFDVQV KRLHEYKRQL LNILHVMYLY NQIKEHPEME FYPRTFIFGA KAAAGYKIAK
LTIKLINSVA DVINNDESIN GKIKVVFIEN YRVSNAEIIF AAADVSEQIS TASKEASGTG
NMKFMLNGAL TLGTMDGANV EIVDEVGEEN AFIFGLSSDE VINYENNGGY NPMDIFNSDM
DIRKVLMQLI NGFYSPDDPE RFRPIYNSLL NTQETDVADR YFILKDFKSY AAAQKRVEEA
YRNEEGWAKS AMLNVANVGK FTSDRTIEEY VQDIWHLEKV KVKMDV
//
