MTNA_BRUA4
ID MTNA_BRUA4 Reviewed; 364 AA.
AC A6X8E9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678};
GN Name=mtnA {ECO:0000255|HAMAP-Rule:MF_01678}; OrderedLocusNames=Oant_4832;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OG Plasmid pOANT04.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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_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:0000255|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:0000255|HAMAP-Rule:MF_01678}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; CP000763; ABS17503.1; -; Genomic_DNA.
DR RefSeq; WP_011983109.1; NC_009672.1.
DR AlphaFoldDB; A6X8E9; -.
DR SMR; A6X8E9; -.
DR STRING; 439375.Oant_4832; -.
DR DNASU; 5383324; -.
DR EnsemblBacteria; ABS17503; ABS17503; Oant_4832.
DR KEGG; oan:Oant_4832; -.
DR PATRIC; fig|439375.7.peg.4995; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_5; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000002301; Plasmid pOANT04.
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; -; 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; Isomerase; Methionine biosynthesis; Plasmid;
KW Reference proteome.
FT CHAIN 1..364
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000357213"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 364 AA; 39764 MW; 47B3DD123D28CDB5 CRC64;
MKVGERHYHT IWLNEDGRSV DIIDQRWLPH EFRVVTLKTV ADVADAIRDM WVRGAPLIGV
TAAYGVAIAM AKDPSDAHLD AVWEELNETR PTAINLRWAL NAMREYLRPL PEAERADAAY
KRAAEIAEED VELNRAIGAN GLDVIREIAS KKKPGEPVRI LTHCNAGWLA TVDYGTATAP
IYMAVEEGIP VHVYVDETRP RNQGAYLTAW EMNGHGVPHT LIVDNAGGHL MQHGDIDMVI
VGTDRTTANG DVCNKIGTYL KALAARDNDV PFYVALPSPT IDWTVQDGVK EIPIEERTAD
EVSFVQGRAA DGSIASVRIS PEGSPAANPA FDVTPARLIT GLITERGIAT PSPEGLKALF
PERS
