ID V5WL69_9SPIO Unreviewed; 841 AA.
AC V5WL69;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=L21SP2_3217 {ECO:0000313|EMBL:AHC16557.1};
OS Salinispira pacifica.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Salinispira.
OX NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC16557.1, ECO:0000313|Proteomes:UP000018680};
RN [1] {ECO:0000313|EMBL:AHC16557.1, ECO:0000313|Proteomes:UP000018680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC16557.1,
RC ECO:0000313|Proteomes:UP000018680};
RX PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA Klenk H.P., Fardeau M.L., Spring S.;
RT "Complete genome sequence and description of Salinispira pacifica gen.
RT nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT mat.";
RL Stand. Genomic Sci. 10:7-7(2015).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP006939; AHC16557.1; -; Genomic_DNA.
DR RefSeq; WP_024269450.1; NC_023035.1.
DR AlphaFoldDB; V5WL69; -.
DR STRING; 1307761.L21SP2_3217; -.
DR KEGG; slr:L21SP2_3217; -.
DR PATRIC; fig|1307761.3.peg.3205; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_12; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000018680; 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW ECO:0000313|EMBL:AHC16557.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000018680};
KW Transferase {ECO:0000256|RuleBase:RU000587, ECO:0000313|EMBL:AHC16557.1}.
FT MOD_RES 670
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 841 AA; 95646 MW; ACFD7304F6880742 CRC64;
MAKASNSAPK NIRNGLDAET VKWDFAETLK YTMGVDSYSA TEHDRYMALA YAVRDRLINQ
WLQTQRTHHD KDVKRVYYLS LEFLMGRAMG NNVINSGIEG AVRKALDELG YDFEELREQE
IDAGLGNGGL GRLAACFIDS MATLDLPAFG YGLRYDYGIF RQEIDNGYQV EHPDDWLRNG
NPWEIERPDI SVEVNFGGRV VATEDNGKIN YRWIDTDSVV GVAYDQPIVG YGGNTVNTLR
LWGARANEEF SFYDFNAGDY AEAVADRVQA ENLTRVLYPN DTLYLGKELR LKQQYFFVAC
SLADIIRRFK KSGKKWTELP KMAAIQLNDT HPSIAVAELM RVLIDEEGLD WDSAWDITVN
TMGYTNHTLM PEALEKWSVP MFEKLLPRHL QLIYEINHRF LSKVAVKFPG DTAKLRDMSI
IEEGEPKMIR MAFLAIVGSH SVNGVAALHT ELLKARLVPN FASMWPERFN NKTNGITQRR
FLLKSNPPLA ELLTETVGDG WITQLSELEQ IRSKAKDATF QKKIAKVKLE AKKRLAEYVE
KDYGYKLDTS HIFDIQIKRI HEYKRQLLNA LHIIMLYNRI KRGDTKDMAP RTFIFGGKAA
PGYQMAKLII KLINNIATVI NNDPDVNKYL QVYFLGNYRV SLAERLIPAA DVSEQISTAG
TEASGTGNMK FMANGALTIG TLDGANIEIK EEAGDDNIFI FGMNADEVEA LRPVYDPYQY
YLEDTEIKEA LDLLFSGYFN FGEPGIFEPI RQTLFERGDN YMHLADLRSY ADAHDQVVKT
YNNQKKWLEM SINNIAGCGK FSSDRTIHQY AEDIWNVKPC KVERNTEGDD TLIEATLKGK
K
//
