ID W0SMC9_9PROT Unreviewed; 851 AA.
AC W0SMC9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:BAO30948.1};
GN ORFNames=SUTH_03175 {ECO:0000313|EMBL:BAO30948.1};
OS Sulfuritalea hydrogenivorans sk43H.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfuritalea.
OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO30948.1, ECO:0000313|Proteomes:UP000031637};
RN [1] {ECO:0000313|EMBL:BAO30948.1, ECO:0000313|Proteomes:UP000031637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO30948.1};
RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA Watanabe T., Kojima H., Fukui M.;
RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT sulfur oxidation pathway of betaproteobacteria.";
RL Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO30948.1; -; Genomic_DNA.
DR AlphaFoldDB; W0SMC9; -.
DR STRING; 1223802.SUTH_03175; -.
DR KEGG; shd:SUTH_03175; -.
DR HOGENOM; CLU_015112_0_0_4; -.
DR Proteomes; UP000031637; Chromosome.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031637}.
FT DOMAIN 14..123
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 851 AA; 96418 MW; 4E350EE8298AED73 CRC64;
MPGTRYQLEV NPEIPARLAR LDELANNLWY SWDRPTRSLF ARLSAGLWRA THHSPKAFLK
RMDQKRINEA ADDPVFLGTM NRVLSAYDSY HSEPRLELPG KPPLQSTDLI AYFCAEFGFH
ESLPIYSGGL GILAGDHCKG ASDLRLPFIA VGLLYRQGYF HQTIDRDGNQ TAHYGDNDFD
DMPIEPMRNQ DGSDVRVGVD FPGRTVWAKV WRARIGINSL YLLDTDLGEN SEADRGIAHQ
LYGGDRRTRI EQEIVLGVGG VRALNALGLN PTVWHINEGH AAFLVLERIR NLVGQNMSFA
AALEAAAANT VFTTHTPVPA GHDHFADDMV MHYFGEFCKA TGLDRDGLLN MGRVGGNGGE
FNMTALALRG SRFHNGVSRI HGEVSSRICG DLWPQVAAAE NPMDYVTNAV HVPTFLATDW
YETFDRHLGL GWQHRLTDQS CWNGVQRIPD QIFWSIRQSL KAQLLHLVHS RVRQQHLRNQ
GSEAHLDRVL RSADPTNPTV LTIGFARRFA TYKRAALLFN NLDWLREILS DAQHPVLFIF
AGKAHPADEP GRRLIRQIAE LSQQREFEGR ILLVEGYDLH LARRMVAGVD VWLNNPIYPL
EASGTSGMKA AINGAINLSV LDGWWGEGYD GKNGWAIKPA AEGLDPAQRD IDEARTLYEL
LQDSVIPMYY RNTSLGYSPE WVAMAKQSIA SIMPRFNMQR MLTDYAEKFY SPAAEQWRRY
SSADFSGARR VADWKARIRA AWPRIGLRRI DQMAARIRYG ETLRFEIAVQ LDGLTPDDLT
VELVFTRPGE PTSARARRYE LHHERPLERG EHLFSRELTP DQCGKMEYRV RVFPTHELLT
HPFEMGMMLW L
//
