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MTNA_UNCRE
ID   MTNA_UNCRE              Reviewed;         386 AA.
AC   C4JWQ7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE            Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_03119};
DE            Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE            EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_03119};
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE   AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000255|HAMAP-Rule:MF_03119};
GN   Name=MRI1 {ECO:0000255|HAMAP-Rule:MF_03119}; ORFNames=UREG_06999;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC       (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC       {ECO:0000255|HAMAP-Rule:MF_03119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC         D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC         ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03119};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 1/6. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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DR   EMBL; CH476618; EEP82134.1; -; Genomic_DNA.
DR   RefSeq; XP_002584032.1; XM_002583986.1.
DR   AlphaFoldDB; C4JWQ7; -.
DR   SMR; C4JWQ7; -.
DR   STRING; 336963.C4JWQ7; -.
DR   EnsemblFungi; EEP82134; EEP82134; UREG_06999.
DR   GeneID; 8442539; -.
DR   KEGG; ure:UREG_06999; -.
DR   VEuPathDB; FungiDB:UREG_06999; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   InParanoid; C4JWQ7; -.
DR   OrthoDB; 1410886at2759; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.420; -; 1.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   HAMAP; MF_01678; Salvage_MtnA; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-M1Pi.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..386
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000402056"
FT   ACT_SITE        258
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            176
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   386 AA;  41716 MW;  EB011A0EB666F41B CRC64;
     MASALEAIKY DRGRLFIIDQ LQLPHVTKFI PIDSSEAGWH AIKAMQVRGA PAIAIVAVLS
     LAVEMLNLVS ENMIPEDGED VRAYIEQKMD YLVSSRPTAV NLSDSAQKIK LLLDQRARKS
     GLSGVETAMA FIQHAEQMLA RDLADNHSIG EYGATWILKN TRAALEGGNT CVLTHCNTGS
     LATAGYGTAL GIIRRLHEHG RLSRAYCTET RPYNQGARLT AYELVSDKIP ATLITDSMAG
     QLLANPDKKI AAIVVGADRV AANGDTANKI GTYTLAVLAK FHNIKFVVAA PRTTIDMKTK
     TGNEIIIEER QSSEVTKIRG PCEGDGDHRE AVMETIKIAA DGIDVWNPAF DVTPAALIDA
     IVTEVGVETK DSSGQFHLSS LFESMA
 
 
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