ID A0A0P9GJ32_9GAMM Unreviewed; 854 AA.
AC A0A0P9GJ32;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Starch phosphorylase {ECO:0000313|EMBL:SCY14697.1};
GN ORFNames=SAMN05661077_1349 {ECO:0000313|EMBL:SCY14697.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdales;
OC Thiohalorhabdaceae; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCY14697.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FMUN01000003; SCY14697.1; -; Genomic_DNA.
DR RefSeq; WP_054966071.1; NZ_LJCP01000010.1.
DR AlphaFoldDB; A0A0P9GJ32; -.
DR STRING; 381306.AN478_07915; -.
DR PATRIC; fig|381306.5.peg.225; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000183104; Unassembled WGS sequence.
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:UP000183104}.
FT DOMAIN 14..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 610
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 854 AA; 97666 MW; 02DDFBCD111A5DF5 CRC64;
MPGTRYRLEV QPRLPESLCR LGELANDLKY TWDRRIRGLF YQLDHVLWEE CSHNPKVFLR
RVSQNRLEQA ARDRVFLEEY NRVLSSFDSY YKEPMRPELQ EHLNQDKDLV AYFCAEFGFH
ESMPLYSGGL GILAGDLVKA ASDMHLPMVA VGILYRQGYF VQTVDAEGNQ VAHYNPTDFD
DLPIEPVRDE DGEEVRVPLP FPGREAWVRI WRARLGHVAV YLLDTDLPDN AEQDRAITYQ
LYGGDATVRI QQEIVLGIGG VRALRALGLR PTVWHVNEGH AAFQALERCR EYVAQGQDLD
TALERTANAT VFTTHTPVSA GHDIFSPDLM GTYFGPYAEE ELGTGMEWLL ALGQDASQDG
GFNMTALAMR TSRYQNGVSR IHGRVASEME GYIWPEIPRG ENPIGYVTNG VHVPTFLARE
WVSFFDLHFG GQWRSELLNE GFWEGIDRIQ DHSFWSVRHS LKAELFAEAR QRLIHQHRRN
GATQAQIERL TEQLHPDRTD VLTIGFARRF ATYKRATLLF TDPDRLARLV NDARRPVLFL
FAGKAHPSDQ PGQHLIRVIH EFSRRPEFEG KIVLLEGYDM ALARKLVTGV DVWLNTPEYP
KEASGTSGQK AGINGGLNLS VLDGWWGEGY NGENGWAITP HDPEMSSDYR NREEAKELLE
LLEDQVVPKY YRRNGHGYSE EWVRMSKNAI KSQIPRFNAQ RMLMDYVRDF YGPASRQQRR
LARAGGEPAQ DLARWKRRVD QAWDQVRVER LDDVREELTS GDSLPITVAV QLNGLSPEDV
RVECLVGRAD DLGDFEARER HGLVPLEEPG PDGATLFHLA LEPTLPGLQY YKLRMYPYHP
ALAHLHETGH MRWL
//
