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 27-MAR-2024, entry version 42.
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 GeneID; 9525504; -.
DR KEGG; abe:ARB_03491; -.
DR eggNOG; KOG4754; Eukaryota.
DR HOGENOM; CLU_039184_0_1_1; -.
DR OMA; CDRRSTA; -.
DR OrthoDB; 1456057at2759; -.
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; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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
//
