ID H2ANM8_KAZAF Unreviewed; 414 AA.
AC H2ANM8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=KAFR0A05430 {ECO:0000313|EMBL:CCF55978.1};
GN Synonyms=MRI1 {ECO:0000256|HAMAP-Rule:MF_03119};
GN ORFNames=KAFR_0A05430 {ECO:0000313|EMBL:CCF55978.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF55978.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF55978.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE650821; CCF55978.1; -; Genomic_DNA.
DR RefSeq; XP_003955113.1; XM_003955064.1.
DR AlphaFoldDB; H2ANM8; -.
DR STRING; 1071382.H2ANM8; -.
DR GeneID; 13886429; -.
DR KEGG; kaf:KAFR_0A05430; -.
DR eggNOG; KOG1468; Eukaryota.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; H2ANM8; -.
DR OrthoDB; 4853at2759; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000005220; Chromosome 1.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000005220}.
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03119"
SQ SEQUENCE 414 AA; 45782 MW; AE7C8315184862FE CRC64;
MSLQSIIFEK SDRTNVLVQV LDQLLLPYTS KYVPIYTIDD GYTVIKNMQV RGAPAIAMVG
ALSVLLETQL LTNKNFTATQ FFYDVSSWAP IRTRLTERLE FLLSSRPTAV NLSNALKDIS
SILHNCEDLT SFNSEVFDYT CKLLDEDSTN NKKMGDNGAE YLLKSLEMEN FAEDFAVLTI
CNTGSLATAG YGTALGVIRS LWKDSVAKTD LSQSPKKIKS GKPRLAHVYP LETRPYNQGS
RLTAYELVHD EIPCTLITDS SIAYRIKTSD VPIKAAFVGA DRIVRNGDTA NKIGTYQLSI
LCKQFGIKFF VVAPKTTIDS VTETGDGIIV EERKPEEFKL VTGTLIDNNG GIMRPAMNEN
NEPINAQVGI APPNAQVWNP SFDVTPHEFI DGIVTEEGVF VKNSQGNFDL QALF
//
