ID A0A093Z520_9PEZI Unreviewed; 454 AA.
AC A0A093Z520;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000256|HAMAP-Rule:MF_03119};
GN Name=MRI1 {ECO:0000256|HAMAP-Rule:MF_03119};
GN ORFNames=V492_03899 {ECO:0000313|EMBL:KFY12396.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY12396.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY12396.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY12396.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_03119}.
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:KFY12396.1}.
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DR EMBL; JPJU01001266; KFY12396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Z520; -.
DR STRING; 1420902.A0A093Z520; -.
DR HOGENOM; CLU_016218_1_3_1; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000029299; 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; translation initiation factor eif-2b, domain 1; 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 NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR00512; salvage_mtnA; 1.
DR PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR43475:SF1; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03119}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03119};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03119}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03119};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
SQ SEQUENCE 454 AA; 49296 MW; B9A5C9014ED288E5 CRC64;
MSALQAIKYT RGKLEVLDQL RLPHESVYDD VSTCEQAFDC IKSMRVRGAP AIAIVAALAL
AVELANADLN QSSVDGQLKY VHDRLDYLMG SRPTAVDLSN AIRLLKMTVN AAAIAEADET
ANKTAKPDAA LIREAYIKAA EKILEDDLQT NLAIGRYGAE YLRRQQLPVL SPDDDADDLR
YFTTSPPGTQ GAPDRTYRKL SVLTHCNTGS LATSGHGTAL GIIRSLHKMN YLDHAYCTET
RPYNQGARLT AFELVYEKIP STLITDSMAG ALFARLKTEK NIAAVIVGAD RVARNGDTAN
KIGTYSLAVL AKFHGVKFIV AAPTTSIDLE TVTGADIVIE DRPQKELTQI SGAVVDKEGN
VDVSDTRRVA VAHQGIDVWN PSFDVTPHAL IDAIITEKGE VVRSANGTFN FQHIMPARWK
QQVEKTEPVD VSALSGKASV ADSEDGTQFK LELV
//
