ID I0Z044_COCSC Unreviewed; 1818 AA.
AC I0Z044;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 13-SEP-2023, entry version 50.
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 ORFNames=COCSUDRAFT_65695 {ECO:0000313|EMBL:EIE24013.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24013.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE24013.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE24013.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the ARR-like family.
CC {ECO:0000256|ARBA:ARBA00010330}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000256|ARBA:ARBA00010165}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:EIE24013.1}.
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DR EMBL; AGSI01000006; EIE24013.1; -; Genomic_DNA.
DR RefSeq; XP_005648557.1; XM_005648500.1.
DR STRING; 574566.I0Z044; -.
DR GeneID; 17042011; -.
DR KEGG; csl:COCSUDRAFT_65695; -.
DR eggNOG; KOG1468; Eukaryota.
DR eggNOG; KOG1601; Eukaryota.
DR OrthoDB; 4853at2759; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000007264; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:InterPro.
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 GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 1.20.120.420; translation initiation factor eif-2b, domain 1; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR010402; CCT_domain.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR009212; Methylthioribose_kinase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR NCBIfam; TIGR01767; MTRK; 1.
DR NCBIfam; TIGR00512; salvage_mtnA; 1.
DR PANTHER; PTHR34273; METHYLTHIORIBOSE KINASE; 1.
DR PANTHER; PTHR34273:SF2; METHYLTHIORIBOSE KINASE; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF06203; CCT; 1.
DR Pfam; PF01008; IF-2B; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51017; CCT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03119}; Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW 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};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03119, ECO:0000256|PROSITE-
KW ProRule:PRU00357}; Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1818
FT /note="Methylthioribose-1-phosphate isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003637388"
FT DOMAIN 752..875
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1602..1644
FT /note="CCT"
FT /evidence="ECO:0000259|PROSITE:PS51017"
FT REGION 909..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1706
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
FT SITE 133
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
SQ SEQUENCE 1818 AA; 190701 MW; B7DE752902BE625B CRC64;
MAVRGAPAIA IAAALALAAE LVNQGGGAQF ESAQAAYQKI TEQLEYLVTS RPTAVNLQIA
ANRLSAIAKK EASVEGGSGV SVTIAVISAA DAMFKDDITA NKTMGKLGAE GILAELASRG
GSSGAGVRVL THCNTGSLAT AAYGTALGVV RALHAAGHLQ HAFCTETRPY NQGSRLTAYE
LVHDGLPAML IADSAAAALM AQRKVDAIVV GADRIAANGD TANKIGTFSL AVNAAHHGIP
FYIAAPTMTV DPSLPDGTLI PIEERSSTEL THHQGQRVAA PGINVWNPAF DVTPASLITG
IITEQGIIQQ RDGAIDVNSF LREHGLLEAE ESRDNGAVTS VPTSKIPGFR ALNLETVKEY
VAERPDLGER VGPSGSKDSW TVREVGDGNI NFVYIVEGPS GALVVKQGLP YIRIAHDWPL
TQERARFEAE ALREEARHCP EHIPELYHFD AALCLLVMQY LPPPHLVLRP ALTAGHSFPS
LARHIAHFMA TTLFRTSLLA LDSKAWRELV GRFENMDICR LTEQVIFTDP YYSAPMNRHT
SPQLDDLADA FQHDVAAKAA IAALKAKFVQ QRQALLHGDL HTGSLMVTAD TTYVIDAEFA
FAGPIAFDVG KMVANLLIAF FAGGGLQTAE QPRTAQRRWL LQATVEMWEL FKTEFRELWN
AALKDKKAGD LCPAPLFGND APAGPDALQA VQEAFFAGLL PDVLGFAGAV IIRRILGIAH
VVDYESITDV DARHPGGAGA AAVDILSPQS LRVLVVDSKA SARQEVVALL RKCTYQVMEV
KSTAEALQLL KDQQARDGAP GVDLILKEHD PPAANACRLL RRTLEDDVLR TVPVVVMSSQ
EDRDVMVACL QLGAADYMIR PLRHNELRNL WARVYWWRRA FYLQQQATHA LGAKEHSLPG
LKLRYYPSLS QSSDESEETK RCQQALKPVN REEMERSGEG SAPNGSGNGG ANGSGNCSKD
GNGNSRVHPG SGGNGNGNSA TKQCEGSNQP NGESGNNGNG DSATKAGNLH FGNGNSGNDA
STSRQEVAAL QGTAQGGKRY RMAQEAGAEM RGAKCEGGAE AGMEPKLWPA DGVRPVKLYR
GGHSRSDAVN DNGNGVVGST TGGQAATLPG SSSRQDSKPN GTNGGDGSSG QDTGNGNGAM
TANGNGGSTS HRMELPSSAE GAQTGGPHQS TRLHSEAGGF RAYIGQAHKR KASEIATVSE
VPLNRASSQA LARNSTAAPR PADCTEAGSM ARAGGAASNT LGPQTTGSTP TSASEDTRMV
GSDGKGTSMP LRLGSKSGSL DQVQVQWPHN ESAQMQQRLQ ASAQRQNSGP APQMPGFRGP
GNFNYFGMPP PNFPMPGPFW PGMPNPMGQV SGQSSGQGSG QGGFQEGNPQ FDAFFGPFGA
QQMAAAMAAA AGAASTGNRE REAAAAAAQQ QQQQQHHFAM ILQQQQAQQQ QMFLQQYGLA
ASNMMQQMAA GGPWQQSNRA QPGSPSAAAA AQFAAAFPFG NPNGSGGARS VPSYPAHPMA
SRGGPMQQYA AARAAAAATA ASNGARPGLM HSAPAAAAGN AGATHGGAGV NNGATSRAPP
GLQQNGTQQN GAEEDAQIGV KAEQGADVLT SGTANATGRE RRMQALHKYK QKRKNLNFTK
KIRYESRKQL AQARPRVKGQ FVRMASGAID ADAVEAAVEA DAAEMLGDLP NLAAAADAAL
AAAKVAAEDE GMDFQDDDES VDNEEEIKEE AAAKWQAGAA QPPEEDDDDN VVNSPQDIFN
RVAGPASNSH GQHSGSRLQS HGIAMHPHSN SNRTASPVVV SNTHGKVAVN GNGSSDSGSN
SPDIKDGPGE SPDADMEQ
//
