(data stored in ACNUC1104 zone)

SWISSPROT: D6ZZY1_STAND

ID   D6ZZY1_STAND            Unreviewed;       305 AA.
AC   D6ZZY1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS01159384};
DE            EC=2.1.2.9 {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS01159356};
GN   Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182};
GN   OrderedLocusNames=Snov_0058 {ECO:0000313|EMBL:ADH87395.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87395.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87395.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of
CC       methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC       in the initiator identity of N-formylmethionyl-tRNA by promoting
CC       its recognition by IF2 and preventing the misappropriation of this
CC       tRNA by the elongation apparatus. {ECO:0000256|HAMAP-
CC       Rule:MF_00182, ECO:0000256|SAAS:SAAS01159395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC         (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC         tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952,
CC         Rhea:RHEA-COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:78530, ChEBI:CHEBI:78844;
CC         EC=2.1.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00182,
CC         ECO:0000256|SAAS:SAAS01159357};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|HAMAP-
CC       Rule:MF_00182, ECO:0000256|SAAS:SAAS01159355}.
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DR   EMBL; CP002026; ADH87395.1; -; Genomic_DNA.
DR   RefSeq; WP_013164900.1; NC_014217.1.
DR   STRING; 639283.Snov_0058; -.
DR   EnsemblBacteria; ADH87395; ADH87395; Snov_0058.
DR   KEGG; sno:Snov_0058; -.
DR   eggNOG; ENOG4105CAE; Bacteria.
DR   eggNOG; COG0223; LUCA.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; GITTMLM; -.
DR   OrthoDB; 2009156at2; -.
DR   BioCyc; SNOV639283:G1GLM-58-MONOMER; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   Gene3D; 3.10.25.10; -; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZZY1.
DR   SWISS-2DPAGE; D6ZZY1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00182,
KW   ECO:0000256|SAAS:SAAS01159369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00182,
KW   ECO:0000256|SAAS:SAAS01159400, ECO:0000313|EMBL:ADH87395.1}.
FT   DOMAIN        1    177       Formyl_trans_N. {ECO:0000259|Pfam:
FT                                PF00551}.
FT   DOMAIN      204    296       Formyl_trans_C. {ECO:0000259|Pfam:
FT                                PF02911}.
FT   REGION      110    113       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   305 AA;  32038 MW;  CA7FC4B84161AD33 CRC64;
     MRIVFMGTPD FAVSTLAEIV GSGHEVVAAY TRAPAASGRR GLELVPSPVH RAAEKLGVPV
     LTPSTLRTEE AAETFAAHEA DVAVVVAYGR ILPQMILDAP KLGCLNLHAS LLPRWRGAAP
     IQRAIMAGDA ESGVAVMKME AGLDTGPVGL VERVAIGADM TAGELHDRLM IVGADLMGRA
     LAALERGALN FTPQPEAGVT YAAKIDKGET RIDWSKPAKQ VHDHIRGLSP FPGAWFEFDG
     VRVKVLRSTL VAGAGRPGEV IDDQLTIACA DGAVRLTEVQ KAGSKAMGAA DFLRGNELTR
     GTVLA
//

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