ID   A0A0U5AXU8_9BACT        Unreviewed;       844 AA.
AC   A0A0U5AXU8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:BAU23279.1};
GN   ORFNames=THC_0894 {ECO:0000313|EMBL:BAU23279.1};
OS   Caldimicrobium thiodismutans.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX   NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23279.1, ECO:0000313|Proteomes:UP000068196};
RN   [1] {ECO:0000313|EMBL:BAU23279.1, ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|EMBL:BAU23279.1,
RC   ECO:0000313|Proteomes:UP000068196};
RX   PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring, and emended description of the genus
RT   Caldimicrobium.";
RL   Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN   [2] {ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU23279.1; -; Genomic_DNA.
DR   RefSeq; WP_068513912.1; NZ_AP014945.1.
DR   AlphaFoldDB; A0A0U5AXU8; -.
DR   STRING; 1653476.THC_0894; -.
DR   KEGG; cthi:THC_0894; -.
DR   PATRIC; fig|1653476.3.peg.928; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000068196; 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; 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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068196}.
FT   DOMAIN          13..120
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         602
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   844 AA;  98636 MW;  6692F8A11E6D8179 CRC64;
     MEFKKFFVYP RFPESLEKLV TISYNLWFTW DFDALSLFYR MDAELFRKVK HNPIKFIHLL
     SKEKIEALAQ DRRFLLDLQE IWERFEEYQK KVHPMVSASD LTKGDVIAYF STEFALHEAL
     PVYAGGLGVL AGDILMGASD LDIPLVGVSL LYNRGYFKQT FDPAGLQKEE SDIFDKFLNI
     LREVKDPEGK PLLIELHILD KFYKAKVWKV EVGKRICLFL DTDIPENPPD VRAITEYLYP
     AEPEKRLKQE ILLGMGGYQA LRKMGLDPKI YHLNEGHSAF VILSRLKELM LEKGLSYPEA
     KLFIQETTVF TTHTPLIAGN EHFDTKLVEK YLGPEVSALG LTMEDLTKCG CILGDKSLFW
     LPALAIRYSR HVNAVSKLHQ ETTKKMWQPL FEDWLFEEVP IDYVTNGVHW RWLSEPFNDL
     LKEYVGLDFR FLGPDDPAWD EILNIPDEEV WEAHKKNKQR LINLLNKLLE EELMRGDPQK
     TSRKWSLPLK RFHLIIGCAR RVTGYKRNNL ILFDKERLLK ILQDTDKPVL FVFAGKAHPK
     DLEGKKMIQE LLDFRAKYQL EDKFVFIENY DLHLARYIIW GSDVWLNNPY RPMEASGTSG
     MKAAINGVLN LSVLDGWWAE GYDGTNGWAI YPKEGLPPYN YFEANQIYTL LEGEIRNLYY
     QRDEEGIPRE WVQRMKRALY ICCKNFSMNR VLLEYLQKFY QPALTQFKTL TAENFALVKR
     LDAERKILEE NWGKIKILSF QTNILGEATW EDSEIEIKVE VEFGDLPKEL VTVELVCIKE
     MGLEEEISKE FTFVPLELEK AENGKAFYSI KYQLYGHGLR KVGVRVVPSN EILRRAYPEL
     IKWY
//