ID A6Q9S2_SULNB Unreviewed; 708 AA.
AC A6Q9S2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=SUN_1278 {ECO:0000313|EMBL:BAF72231.1};
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum.
OX NCBI_TaxID=387093 {ECO:0000313|EMBL:BAF72231.1, ECO:0000313|Proteomes:UP000006378};
RN [1] {ECO:0000313|EMBL:BAF72231.1, ECO:0000313|Proteomes:UP000006378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1 {ECO:0000313|EMBL:BAF72231.1,
RC ECO:0000313|Proteomes:UP000006378};
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
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DR EMBL; AP009179; BAF72231.1; -; Genomic_DNA.
DR RefSeq; WP_011980964.1; NC_009663.1.
DR AlphaFoldDB; A6Q9S2; -.
DR STRING; 387093.SUN_1278; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; sun:SUN_1278; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_7; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000006378; 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:UniProtKB-KW.
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 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 ECO:0000313|EMBL:BAF72231.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAF72231.1}.
FT DOMAIN 15..118
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 604
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 708 AA; 81685 MW; 5694DAF9886941C2 CRC64;
MFIDDPSKNI AIPKLPKEIE FLSDIALNLW WTWNPRGKNL FKLINPYLWK ESSENPIKML
NALSRKDLAS LGEDETFMKE YKYVHALFKD YMQDSRVYAE EEPLPIAYFC AEYGLHHSVP
IYSGGLGFLA GDILKESSDM GLPMVGIGFM YAQGYVRQVI GSDGWQNGSN ETIDKDSAPI
ERVLDHDGNH FTIQVPFIDP PVYTSVWKIN VGRVTLYLLD TDVEQNDPWD RGISSHLYVP
DMNQRLRQQI VLGIGGYRVL EELGIKYSIL HLNEGHPAFA LFERVRSFIE DEKMSLDEAV
EKVKETSVFT THTPLQAATD VYSFDMMSNY FRDYWQKLGL SKEQFFSFGS NPDAPNDGFN
MTVLGLKMCH QRNAVSKKHS EVTKEIWKNV FAMDTKENVP IEYVTNGVHI PTWLSDELTR
TYDKVLGEQW QHLEDEEAVW SRVEEIDEEK IWDMHYANKV RLVNFVRERV RQKWANEGID
PLVAMAEGVM LDPDVLTIGF ARRMTSYKRP NLILHDLEKL EKIVIDCDRP VQIIFTGKAH
PSDNPGKKMI QNIFKVAQNP RFKGRIAFIE DYGEEVAKYL VRGVDVWLNN PQIPMEACGT
SGMKASLNGT LHFSGLDGWW PEAYNGENGW KIGKEISDDA RDAQDIYDIL ENEIVPLFYN
IDNEAFPKEW VKKMKKAMMS ISPQFSARRM MKDYLDKFYI PIGKKIKE
//
