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Database: UniProt
Entry: A0A1T2KU74_9GAMM
LinkDB: A0A1T2KU74_9GAMM
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ID   A0A1T2KU74_9GAMM        Unreviewed;       352 AA.
AC   A0A1T2KU74;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE            Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678};
DE            Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE            EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678};
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN   Name=mtnA {ECO:0000256|HAMAP-Rule:MF_01678};
GN   ORFNames=BOW51_07550 {ECO:0000313|EMBL:OOZ36341.1};
OS   Solemya velesiana gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918948 {ECO:0000313|EMBL:OOZ36341.1, ECO:0000313|Proteomes:UP000190896};
RN   [1] {ECO:0000313|EMBL:OOZ36341.1, ECO:0000313|Proteomes:UP000190896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Se-Cadez {ECO:0000313|EMBL:OOZ36341.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) 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_01678}.
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_01678};
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_01678}.
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
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:OOZ36341.1}.
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DR   EMBL; MPRJ01000043; OOZ36341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2KU74; -.
DR   OrthoDB; 9803436at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000190896; Unassembled WGS sequence.
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|HAMAP-Rule:MF_01678};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190896}.
FT   ACT_SITE        244
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         56..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   SITE            164
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   352 AA;  37245 MW;  36EFAC73030B97F3 CRC64;
     MQTIPLDIQA DADHAIVWAN DRLYLLDQRV LPAEESYLEL QSAEQTATAI SDMVVRGAPA
     IGITAAFGVV LAGRRCYAEF GGDWKSHIHS ELDTLAASRP TAVNLFWALK RMKRLIADMG
     AEDPVPSLLS EARKIHEEDI AANRTMGEFG AGLIEGPTSV ITHCNAGALA TGGYGTALGV
     IRSAHAAGKI EMVYADETRP WLQGSRLTAW ELARDNIPVT LLTDGAAASR MAWGGVGWII
     VGSDRIAANG DVANKIGTYS LAVAARHHGV KVMVAAPTST IDMNVASGAD IPIESRDPAE
     VLCCGGRQVG AADVPAWNPV FDVTPAALVD AIVTEKGVVR LPDTKKMADL MT
//
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