ID B6AP13_9BACT Unreviewed; 862 AA.
AC B6AP13;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=Glycogen phosphorylase {ECO:0000313|EMBL:EDZ38880.1};
GN ORFNames=CGL2_11276047 {ECO:0000313|EMBL:EDZ38880.1};
OS Leptospirillum sp. Group II '5-way CG'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ38880.1};
RN [1] {ECO:0000313|EMBL:EDZ38880.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14961025; DOI=10.1038/nature02340;
RA Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT "Community structure and metabolism through reconstruction of microbial
RT genomes from the environment.";
RL Nature 428:37-43(2004).
RN [2] {ECO:0000313|EMBL:EDZ38880.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA Banfield J.F.;
RT "Population genomic analysis of strain variation in Leptospirillum group II
RT bacteria involved in acid mine drainage formation.";
RL PLoS Biol. 6:E177-E177(2008).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; DS995260; EDZ38880.1; -; Genomic_DNA.
DR AlphaFoldDB; B6AP13; -.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1}.
FT DOMAIN 27..130
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 616
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 862 AA; 97335 MW; 7B59971CCE28C431 CRC64;
MAFFDDIPSG GDDTTSFCLP HTDVEGFDRL VRLALDLRWS WNHAADTLWR KLDPVLWELT
HNPWALLQTI SREKVERVLS DPGVKEELDR LSEARRLADL EPGWFHRAFS GSALDHVAYF
SMEFMLSEAL PIYSGGLGNV AGDQLKAASD LGVPVVGIGL LYQQGYFHQS IDSDGNQTAL
FPYNEPGQLP ISPVRKPNGE WVRFTIELGR EKLWLRVWKV RVGKVFLLLL DTNDLANTSS
QREITSELYG GNSTLRLQQE VVLGIGGWRC LDALGIKASV CHLNEGHAAF ALLERARIFM
KSYEVGFDEA LAATRAGNLF TTHTAVPAGF DRFPPDLVLR FLGPYAGDHL GLSPETFLAM
GRLNPTDPGE PFNMAYLALR GSGRANGVSR LHGQVSREIF SPLFPRWPFE EVPVGHVTNG
VHVPSWDSAE ADALWTRFCR KDRWLGTLET MGEEVDQIPD PELWEFRNSS RKSLIEFVRH
RCTREGLQSG KISRGQEEAQ NLLDPFVLTI GFSRRFATYK RPNLLLLNPE RLVRLLNDPH
RPLQLLVAGK AHPQDGAGQA LVREWITFTK RPDVRGKAIF LEDYDMLLAE RLVQGVDLWV
NTPRRPWEAC GTSGMKVLVN GGLNLSELDG WWAEAFDPKS GWAIGDGQDH GDDPVHDHAE
ADELFDRLEQ EILPLFYERD GRGIPAGWVE RMRKSMGTLT PRFSANRAVR EYTTSHYFPA
AETFRIRSEN QASVAREIVR KTRLWEKGWN TLSFGEYSVT VQEGLHLFTV RIHPGILPPD
SLKVELYAAP EGTKPAEHHP MEWVTENSLQ KDQGKKRNPN GWRTCRVQIP LLRPVGDYTP
RILPAFEGLS VPLEAGWIAW QR
//