MTNA_ANOGA
ID MTNA_ANOGA Reviewed; 351 AA.
AC Q7PKS9; Q8T5K0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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 ORFNames=AGAP001589;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12060762; DOI=10.1073/pnas.082235599;
RA Thomasova D., Ton L.Q., Copley R.R., Zdobnov E.M., Wang X., Hong Y.S.,
RA Sim C., Bork P., Kafatos F.C., Collins F.H.;
RT "Comparative genomic analysis in the region of a major Plasmodium-
RT refractoriness locus of Anopheles gambiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8179-8184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD27760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ439060; CAD27760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAAB01008987; EAA43149.1; -; Genomic_DNA.
DR RefSeq; XP_321518.1; XM_321518.4.
DR AlphaFoldDB; Q7PKS9; -.
DR SMR; Q7PKS9; -.
DR STRING; 7165.AGAP001589-PA; -.
DR PaxDb; Q7PKS9; -.
DR GeneID; 1281584; -.
DR KEGG; aga:AgaP_AGAP001589; -.
DR VEuPathDB; VectorBase:AGAP001589; -.
DR eggNOG; KOG1468; Eukaryota.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; Q7PKS9; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; Q7PKS9; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000007062; Chromosome 2R.
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; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
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..351
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000401973"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ SEQUENCE 351 AA; 37951 MW; 3781E39C9706AF3C CRC64;
MTLEAIKYKS GQLQILDQLL LPAESKYIPV AGVKDGWSAI HKMQVRGAPA IAIVGCLSLV
VEIYDKQYET KAALANEIGE HLQYLVTSRP TAVNLKLAAD DVKGQVESLL ANETVTVDGM
KQEVIKAIEY MLEKDISDNR AIGDNGANVL VKGVDRPLKL LTHCNTGSLA TAGYGTALGV
IRSVNERNLL EHVYCTETRP YNQGARLTAY ELVHDKLPAT LVTDSMVAAL LNSRKIDAII
VGADRVAANG DTANKIGTYQ MAVVAKHHGV PFYVAAPFTS IDVAIEDGSH IKIEERPEHE
LTHIGGQRIA APGIGCWNPA FDVTPAELIT GIITERGVLK PCELAEKVRQ K
