ID V4NCF8_9CAUL Unreviewed; 814 AA.
AC V4NCF8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=ABAC402_17270 {ECO:0000313|EMBL:ESQ73796.1};
OS Asticcacaulis sp. AC402.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282361 {ECO:0000313|EMBL:ESQ73796.1, ECO:0000313|Proteomes:UP000017812};
RN [1] {ECO:0000313|EMBL:ESQ73796.1, ECO:0000313|Proteomes:UP000017812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC402 {ECO:0000313|EMBL:ESQ73796.1,
RC ECO:0000313|Proteomes:UP000017812};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ73796.1}.
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DR EMBL; AWGC01000038; ESQ73796.1; -; Genomic_DNA.
DR RefSeq; WP_023450970.1; NZ_AWGC01000038.1.
DR AlphaFoldDB; V4NCF8; -.
DR STRING; 1282361.ABAC402_17270; -.
DR PATRIC; fig|1282361.3.peg.3366; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000017812; 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:UP000017812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 814 AA; 90688 MW; 29D77D43F2DC315E CRC64;
MSVSKGPLEI ALEAEAPIDL ADRIIDALRY RIGKDRQAAR PHDWLAATVL TVRDRVIDKW
MASTRNAHAS GAKRVYYLSL EFLIGRLLRD ALSNLGVMEE VRAALSSLDV DLEIIREIEP
DAALGNGGLG RLAACFMESL ASLDLPAYGY GIRYVNGMFR QRIDDGWQVE LPETWLEYGN
PWEFERRESA YHVGFGGEVI ADEAALAKWV PGEQVIAMAV DTPVVGYGGK RVNTLRLWNA
HAIDPIRLDA FNAGDHIGAL AGKNRAESLT RVLYPADSSS AGQELRLRQE YFFSSASLQD
ILRRHIQYFG DIRTLPDKAA IQLNDTHPAV SVAEMMRLLI DVHNLGFEEA WKITVATFGY
TNHTLLPEAL ESWPLALFER LLPRHTQLIY AINANVLKAA RKVRPDDDAF VAAISLIDER
GDRRVRMANL AFAGSHSVNG VAALHTQLMK ETVFADLNTL YPNRINNKTN GITPRRWLQQ
CNPRLTSLIR EAIGDSFLAR AENLTDLDAF ASDAAFQEKF AAVKRHNKVD LSEYLRRTLG
IKTDPDAMFD VQIKRIHEYK RQLLNILETV ALYNQIRLHP ERDWTPRVKI FAGKAASSYH
RAKQIIKLAN DVARRINADP AVGSLLKVAF IPNYNVSLAE LIVPAADLSE QISTAGLEAS
GTGNMKFALN GALTIGTLDG ANIEIRDRVG DDNIFIFGMT ADQVAARRAE GYDPAAAINA
SPELAQALAN IGSGVFAPDD PARYTDLVHD LFHSDWFMVA ADFDAYERTQ RRIDKVFQHS
AIWTEKAVHN TANMGWFSSD RTIQQYAADI WGMI
//
