ID A3VFV6_9RHOB Unreviewed; 790 AA.
AC A3VFV6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 13-SEP-2023, entry version 61.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=RB2654_06469 {ECO:0000313|EMBL:EAQ12732.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ12732.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ12732.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ12732.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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 -!- 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 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ12732.1}.
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DR EMBL; AAMT01000007; EAQ12732.1; -; Genomic_DNA.
DR RefSeq; WP_008329875.1; NZ_VNHV01000013.1.
DR AlphaFoldDB; A3VFV6; -.
DR STRING; 314271.RB2654_06469; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_5; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000002931; Unassembled WGS sequence.
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 InterPro; IPR035090; Pyridoxal_P_attach_site.
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.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 639
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 790 AA; 89657 MW; BF3073921CF62F5E CRC64;
MTTPSFRESI LRHLTYSFGK DPDHAILEDW RMALSLGVRD RIVDAWFKST KRTYETGAKR
VYYLSMEYLI GRLLEDGLVN LELVDEAREV LAEFGYDYDT VLADEPDAAL GNGGLGRLAA
CFMESLSTIG CPAHGYGIRY EHGLFRQSFV DGRQIEQPEL WLGQRHAWEF ERPEVRYRIG
FGGHVDVRDG HYRWHPGEEV EAEAFDTPTV GWKGRWANTL RLWSGRAIHP FDLEAFNHGD
FTRAAAPEAL ARTISRVLYP DDTTEQGREL RLKQEYFLTA SALRDILRRF SNQFDDLRKL
PEKVAIQLND THPAIAGPEL IRILVDEKGF DFDEAMEIAQ GCLSYTNHTL LPEALEAWGE
QLFGRLLPRH IGIIDRIDAT HAGRNPSRTQ SMRADQSVKM GQLSFVMAHK VNGVSALHTD
LMKTTVFSEL HGLHPDRIVN QTNGVTPRRW LLSCNPGLAG LITESIGEDW VDDLEQLSKL
EPFIDDAGWL EHFDAVKRDN KVWLSNWMRD TYGMHADPDA LFDVQIKRIH EYKRQHLNIL
ETIALWQEMR ENPNADWTPR LKLFGGKAAP GYFFAKDIIR LINDAASVIN NDPLTQGMLR
IAFLPNYNVS LAERMIPAAD LSEQVSTAGK EASGTGNMKL ALNGAPTIGT LDGANVEIRE
RVGADNFFLF GMTAQEVEDR RRVEGHAGLA IAADDRLKGA LDLIRDGRFS PGETDRYRGI
TENLEGPDYF LVCSDFTDYW RAQREVDVVF RDDKAWDRMA ALNTARSGWF SSDRTIRGYM
ADIWNAESLL
//
