ID N1V7L7_9MICC Unreviewed; 875 AA.
AC N1V7L7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:EMY34233.1};
GN ORFNames=D477_010726 {ECO:0000313|EMBL:EMY34233.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY34233.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY34233.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY34233.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
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}.
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:EMY34233.1}.
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DR EMBL; ANPE02000125; EMY34233.1; -; Genomic_DNA.
DR RefSeq; WP_005268978.1; NZ_ANPE02000125.1.
DR AlphaFoldDB; N1V7L7; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000010729; 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:UP000010729}.
FT DOMAIN 13..119
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 875 AA; 96782 MW; 7AAB58CE977985A1 CRC64;
MKAIRRFTVR TVLPEPIAPL ARLAGNLRWS WHQPTQQLFE RLDPKQWRRS HDPVALLGSF
NREQLHELAA DKDLVARVRE VSEDLDRYLT GARWYQGLGA EAPKSIAYFS PEYGIASVLP
QYSGGLGILA GDHLKAASDL GVPLIGVGLL YAAGYFKQSL SRDGWQQETY PLLDPDGLPL
TLLREPDGTP AQVELPLPND RVLLANIWRA DVGRVPLLLL DSNVAGNDDA ARHITDRLYG
GGGDHRLQQE LLLGMGGVKA LRIFQRLTGC EAPEVFHTNE GHAGFLGIER IRELMDEGLS
WEEALAAGRA NTVFTTHTPV PAGIDRFEKL QVAHFFRAGL APNVPTDKIL ALGEENYSGG
DPIKFNMAVM GLRLAQRANG VAKLHGVVSR GMFAGLWPGF DTDEVPISSV TNGVHVPTWV
DPRIAELARD KFGSGSIRER HWDRVYDVSD AEIWTLRREL RGNLIEDVRR RLRSSWKKRG
ATDAELAWTD DVLDPDVLTI GFARRVPTYK RLTLMLRDPA RLKALLLHPE RPIQLVIAGK
SHPADEQGKR MIQDLVRFTD DPEIRHRIVF LPNYDIAMAR TLFPGCDVWL NNPLRPLEAC
GTSGMKAAIN GGLNLSVLDG WWDEMYDGDN GWAIPTANPS TATGADALFS VDERDDIEAA
ALYDLLENHV APRFYAHEAP EGAGAAGPSE PLASDDRLPH QWIAMIRHTL ANLGPAVSAE
RMLEDYVRGL YTPACSSGRE IRANRFAAAR NLAAWSTRVH HAWRDVAVEH VDSLGMQDVP
QIGDLVRVSA FIRLGLLSPE DVCVEVAHGK VSEGDELLET SFDQLILKED LGDGRYLFSG
EVQIDRSGSF GYTVRVLPYH PSLASKSELG LVTNA
//
