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PMU1_ARTBC
ID   PMU1_ARTBC              Reviewed;         335 AA.
AC   D4B4V1;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Probable phosphoglycerate mutase ARB_03491 {ECO:0000305};
DE            EC=5.4.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_03491;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Probable phosphomutase that may have a function related to
CC       the manipulation of phosphate groups on carbohydrates.
CC       {ECO:0000250|UniProtKB:P36069}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000035; EFE29596.1; -; Genomic_DNA.
DR   RefSeq; XP_003010236.1; XM_003010190.1.
DR   AlphaFoldDB; D4B4V1; -.
DR   SMR; D4B4V1; -.
DR   STRING; 663331.D4B4V1; -.
DR   EnsemblFungi; EFE29596; EFE29596; ARB_03491.
DR   GeneID; 9525504; -.
DR   KEGG; abe:ARB_03491; -.
DR   eggNOG; KOG4754; Eukaryota.
DR   HOGENOM; CLU_039184_0_1_1; -.
DR   OMA; GRHGQGF; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..335
FT                   /note="Probable phosphoglycerate mutase ARB_03491"
FT                   /id="PRO_5003054518"
FT   ACT_SITE        108
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        211
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   SITE            283
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
SQ   SEQUENCE   335 AA;  37547 MW;  625C25628E94CA31 CRC64;
     MAGRILLGLT LLATSLPLLA MGDAAVVPCI SYSTVPGYFL QDDPAVDPKT FDYAKEGFGL
     IDQAYDTDET LDAELKKLPW RRFEHKVRSL NKHAASNVRF AVLFLGRHGQ GFHNVAEAYY
     GTKAWDDYWS KLDGDGTITW SDAHLTEEGI SQAKVARDTW AGQMKNSIPL PEVYYTSPLD
     RCLATAKFTF SKLELPPSKP FIPTVKELLR ETLGVHTCDR RSSRNYIEST YPTYKIEPGF
     TQKDMLWDPE VRESDSDRDA RLKKLLDDIF SHDKSTFMSL TAHGGAIRSI LNVIGHREFG
     LQTGAVIPVL IRIETSTDAP EDPEEDLTIK IQGLN
 
 
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