ID A9BGX9_PETMO Unreviewed; 855 AA.
AC A9BGX9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ABX32560.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:ABX32560.1};
GN OrderedLocusNames=Pmob_1871 {ECO:0000313|EMBL:ABX32560.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX32560.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX32560.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000879; ABX32560.1; -; Genomic_DNA.
DR RefSeq; WP_012209657.1; NC_010003.1.
DR AlphaFoldDB; A9BGX9; -.
DR STRING; 403833.Pmob_1871; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; pmo:Pmob_1871; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000000789; Chromosome.
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:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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 Glycosyltransferase {ECO:0000313|EMBL:ABX32560.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000313|EMBL:ABX32560.1}.
FT DOMAIN 13..122
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 855 AA; 98836 MW; CFECE2CFC6A279D9 CRC64;
MDFISKITVV PKIPEKILGL KELSENMWWT WNYKTQALFE TIDKELWEST QRNPVTFLKR
VEQKKLNTAA EDSKFNELYQ EVMKEFSNYM NENSNTWFSK THRSFKDGEI AYFCMEYGLH
ESFPMYSGGL GILAGDHLKS ASDLGIPLIA IGLLYQKGYF IQRLNSEGWQ ESIFLDYDFS
DFPIIPAKES NGDEIYVDID LLGKKVFAKV WQVKVGRVNL YLLDTNLMQN DPEDREITST
LYGGDIEMRI KQEILIGIGG VKAVRKLGYN PSVWHMNEGH AAFLGLERIR ELVQEHGLTF
QEAIEAVRAG NVFTTHTPVP AGNDVFSISL IDKYFGDFWP KLGASRQDFL NLGLEKRQNA
EELFSMTILA LKLSGRSNAV SRLHGEVSRK LWNHVWPGIE WLEVPINYVT NGVHIDTWLN
PKLQESLKEY LGADWMSKID DPELWEKIDN IPDHELWETH QQLKKELIEY IRKSIKAQRS
RHGETVEQLE EVNQIGDEKA LTIGFARRFA TYKRADLIFS DEERLKKILN DPDKPVQLIF
AGKAHPADKP GQELIKKIYE YSRKPEFQNK VIILENYDMD MARHLVSGVD IWLNNPRRPR
EASGTSGQKA GMNGAINFSV LDGWWVEGYN GKNGWAIGDN RDYEDLKLQD KIDSVSIYNQ
LEKQIVPMYY EKGETDVSKE WVSKMKESIK SVTSFFNTAR MLKEYTQKLY MPALEQHTRF
SNDDFKLAKE FAGWVKLLKE NWDSIKIHVK LDQDLTGVKN AEEEIGVQAE IYLPGIGPDS
ILPEVVFARL KDGKIANIRR YDMKLIKEVQ KDTYLYSVKF KIEDRGEYGI NVRVTPNNPL
MPHKNYLMGL VKYPQ
//
