ID   A0A1M5YEL0_9ACTN        Unreviewed;       557 AA.
AC   A0A1M5YEL0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Phosphoglycerate mutase (BPG-dependent) {ECO:0000313|EMBL:SHI10457.1};
GN   ORFNames=SAMN05444521_3980 {ECO:0000313|EMBL:SHI10457.1};
OS   Streptomyces sp. 3214.6.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHI10457.1, ECO:0000313|Proteomes:UP000190947};
RN   [1] {ECO:0000313|Proteomes:UP000190947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT670819; SHI10457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5YEL0; -.
DR   STRING; 1882757.SAMN05444521_3980; -.
DR   OrthoDB; 9781415at2; -.
DR   Proteomes; UP000190947; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
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; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190947};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        408..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        502..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          535..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         7..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            159
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   557 AA;  59562 MW;  4CE0EA3D5C3BE3A0 CRC64;
     MPLFFLRHGE SQANEQNRFA GRLDTPLTAL GGRQADQAAE RVAALAASGV HIDEVHMSTL
     QRARQTAWTI IDRLPQPPDR ITVGEALTER DFGVYSGRNK SLVKKTIGFA GYTEAFHSPT
     GRPPGGESWR EMYDRVAAYY EDVLLPASRA GRTVLVVAHK YVVEMFALVV ADASPDKYRD
     FKIPNARPLS EQDLRRAVAA PAAAGLVNDL GEIVEIRLPL LVATAAAMGV AVQLALGIQV
     PATVFTTALT PLLAVGSFFA MLRVDPPTLR RPLSSLRAAW PLLLPRLALG LVLIWAGHSL
     PLELAGLFLL LPPALIAPTL SLLWGGDYFF AVRHTVAASL ALPVLLLTGL ALPLSLPGTA
     PTLTLGRLEP ALLAYAAVLL AALVLPGVGA QAVRRRDPIR AGALSTNWNW LGGLALVPVA
     GLATFALTPS VGLTAHTAIR LLLVMSAAAA ALTALRLLTT LFLHLRPHGT GLGRDLFITQ
     NTPNIFLWLA MTAVLAPTTG HRPSVIGLGV ALVFFFAVYT DERIFLHAHR HDLTPSVPEA
     PEKRKNPTIP GLLTPGK
//