ID A0A1Q4YAW3_9ACTN Unreviewed; 240 AA.
AC A0A1Q4YAW3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:OKI31701.1};
GN ORFNames=A6A29_23985 {ECO:0000313|EMBL:OKI31701.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI31701.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI31701.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI31701.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI31701.1}.
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DR EMBL; LWLE01000038; OKI31701.1; -; Genomic_DNA.
DR RefSeq; WP_073729155.1; NZ_LWLE01000038.1.
DR AlphaFoldDB; A0A1Q4YAW3; -.
DR STRING; 1718998.A6A29_23985; -.
DR OrthoDB; 4120859at2; -.
DR Proteomes; UP000186952; Unassembled WGS sequence.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR022492; Phosphomutase_MSMEG4193_put.
DR NCBIfam; TIGR03848; MSMEG_4193; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF2; CONSERVED PROTEIN; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000186952}.
FT REGION 214..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 240 AA; 25133 MW; 0AA0CB76BD760455 CRC64;
MPTLILVRHG RSTANTAGVL AGRTPGVSLD ERGAEQAAAL PGRLSALTLA AAVSSPLQRC
RETLQPLLDA RPGLPLHTEE RISECDYGDW SGRKLAELSD DPLMTVVQQH PSAAAFPGGE
SMRAMQARAV DAVRDWNARI EAEHGDDATY VMCSHGDIIK ALVADALGMH LDLFQRVHAD
PCSVTAIRYT RLRPFLLRLG DTGDFASLAP REQGVGADAA GPPAQDGSAD AAVGGGAGAP
//
