ID S3Z4J0_9MICO Unreviewed; 842 AA.
AC S3Z4J0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=HMPREF1484_01306 {ECO:0000313|EMBL:EPH15670.1};
OS Dermabacter sp. HFH0086.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Dermabacter.
OX NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15670.1, ECO:0000313|Proteomes:UP000014577};
RN [1] {ECO:0000313|EMBL:EPH15670.1, ECO:0000313|Proteomes:UP000014577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15670.1,
RC ECO:0000313|Proteomes:UP000014577};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dermabacter sp. HFH0086.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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:EPH15670.1}.
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DR EMBL; ATFO01000007; EPH15670.1; -; Genomic_DNA.
DR RefSeq; WP_016664216.1; NZ_KE340308.1.
DR AlphaFoldDB; S3Z4J0; -.
DR STRING; 1203568.HMPREF1484_01306; -.
DR PATRIC; fig|1203568.3.peg.1281; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000014577; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014577};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..119
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 609
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 842 AA; 93576 MW; BF799DBAFFCF6A6E CRC64;
MKALRTLSVT SELPAELEGL RTLAYNLRWT WNAETRDLFE ALDPRAYEES NRNPVVQLGM
VPARRYSEVA ADPKFRSALE DCLEDLDTYM TSERWFQKEV PAAPAIAYFS MEFGITPTLP
IYSGGLGILA GDHLKSASDL GVDLIGVGLL YQWGYFSQSL NREGWQQENY KQNVTEDLAV
VPVTDADGDQ VCVNVTFPGE RIITIALWKA QVGRISLLLL DTNVEGNDEG ARQITDRLYG
GDHFHRIEQE IVLGIGGVRA VERFAELEGR RERDVFHLNE GHAGFLGLER IGQLMGKGLS
FDAALTKTRA GSVFTTHTPV PAGIDRFDAG QLRHFLDADG NGISRLVPNL PVEAALALGV
EDGGQIFNMA HMGFRLSQRS NGVAKLHGET SRRMFKDLYP GFDEAEVPIT SITNGVHRRT
WISRPMDALY KSVFGDIDLS ARSDWSQLGT LSDKALLDVR NTLRANLVER AREDVRRSWV
RRGAHPGELG WVDSVLDPNV LTIGFARRVS TYKRLTLMLS QPERLREILL NEERPVQIVV
AGKAHPADYP GKEFMQRLVQ FADDHGVRHR IVFLADYDIR MAQYLVSGSD VWLNNPIRPE
EASGTSGMKV ALNGGLTFST SDGWWDEMAT DDAGWTIETV DIEDRAERDR LEAESLYNIL
ENRIVPLFYD RDESGVPAKW LQMVRNSLME IAPKVTATRM VRDYVEQLYA PASQSVALFA
NDEGLSHEFA EYKQRLAQGW GGVSVREVED SVDGDVLAVS ASVELGEIHA DDVQVQLVVG
SANEDGELED PTTVAMTQGV DGRYAAEHPL ETLGSVGYTV RVVPSHRVLA HTAELGLVHV
AQ
//
