GenomeNet

Database: UniProt
Entry: S5VSS5_STRC3
LinkDB: S5VSS5_STRC3
Original site: S5VSS5_STRC3 
ID   S5VSS5_STRC3            Unreviewed;       566 AA.
AC   S5VSS5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
DE            Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE            EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
GN   Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087,
GN   ECO:0000313|EMBL:AGS71020.1};
GN   ORFNames=B446_21040 {ECO:0000313|EMBL:AGS71020.1};
OS   Streptomyces collinus (strain DSM 40733 / Tue 365).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS71020.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGS71020.1, ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX   PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA   Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT   "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT   Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL   J. Biotechnol. 168:739-740(2013).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC         glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC         COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78520; EC=1.2.1.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00001415, ECO:0000256|HAMAP-
CC         Rule:MF_00087, ECO:0000256|RuleBase:RU000584};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005059, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure with
CC       each monomer consisting of three distinct domains arranged along a
CC       curved 'spinal' alpha-helix. The N-terminal catalytic domain
CC       specifically recognizes the glutamate moiety of the substrate. The
CC       second domain is the NADPH-binding domain, and the third C-terminal
CC       domain is responsible for dimerization. {ECO:0000256|HAMAP-
CC       Rule:MF_00087}.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC       with the formation of a thioester intermediate between enzyme and
CC       glutamate, and the concomitant release of tRNA(Glu). The thioester
CC       intermediate is finally reduced by direct hydride transfer from NADPH,
CC       to form the product GSA. {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006259; AGS71020.1; -; Genomic_DNA.
DR   RefSeq; WP_020941475.1; NC_021985.1.
DR   AlphaFoldDB; S5VSS5; -.
DR   STRING; 1214242.B446_21040; -.
DR   KEGG; sci:B446_21040; -.
DR   PATRIC; fig|1214242.5.peg.4313; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_4_0_11; -.
DR   OMA; FAFKCAA; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000015423; Chromosome.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   Gene3D; 3.30.460.30; Glutamyl-tRNA reductase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR018214; GluRdtase_CS.
DR   InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR   InterPro; IPR036343; GluRdtase_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   NCBIfam; TIGR01035; hemA; 1.
DR   PANTHER; PTHR43013; GLUTAMYL-TRNA REDUCTASE; 1.
DR   PANTHER; PTHR43013:SF1; GLUTAMYL-TRNA REDUCTASE; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR   SUPFAM; SSF69075; Glutamyl tRNA-reductase dimerization domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00087};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00087};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00087}; Reference proteome {ECO:0000313|Proteomes:UP000015423}.
FT   DOMAIN          6..156
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          184..281
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          445..544
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
FT   REGION          278..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   BINDING         114..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   BINDING         192..197
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
FT   SITE            99
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087"
SQ   SEQUENCE   566 AA;  58886 MW;  F9D22D8005D9BB93 CRC64;
     MSLLVVGLSH RSAPVSVLER AALSVDAQAK LVQDTVAAEP ATEAAVLATC NRIELYADVD
     KFHAGVAELS TLLAQHSGVG LEELTPYLYV HYEDRAVHHL FSVACGLDSM VVGEGQILGQ
     IKDSLARAQE LHTAGKLLND LFQQALRVGK RAHSETGIDR AGQSLVTFGL EQLAAGGDVQ
     GWAAGRRALV IGAGSMSSLA AATLARAGVA EVVVANRTFE RAERLARILT EGDDTDVAAR
     AVPMDAVPGE LTRADVVVSC TGATGLVLTA EAVAQAVEDR TGRPAEDEGD DTGTGGTAVA
     ALPPTSLGAE ENCPLDLAAV QGSTGFSVAG EAAVAGMDAA TLEQHAAWVD NGTLDRRARR
     GPEADAELIT ALAATVATVG RIPERRRPEP VAGIPRPAPA LFLLDLAMPR DIDAAAHRLA
     GVRLVDIESL AEASADAPMA ADVDQVRRIV SDEVAAFGAA QRAAHITPTV VALRTMAADV
     VAGEIARLDG RLPDLDERQR GEIRQAVHRV VDKLLHAPTV RVKQLAAEPG GAGYADALRT
     LFDLDPETVA AVSRAGDSTD KKDRPA
//
DBGET integrated database retrieval system