HEM1_BURTA
ID HEM1_BURTA Reviewed; 432 AA.
AC Q2SUG3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087};
DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087};
DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087};
GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; OrderedLocusNames=BTH_I2929;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00087};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00087}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00087}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC36831.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000086; ABC36831.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_009888666.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2SUG3; -.
DR SMR; Q2SUG3; -.
DR EnsemblBacteria; ABC36831; ABC36831; BTH_I2929.
DR KEGG; bte:BTH_I2929; -.
DR HOGENOM; CLU_035113_2_2_4; -.
DR OrthoDB; 1358620at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000001930; Chromosome I.
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 Gene3D; 3.30.460.30; -; 1.
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 Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1..432
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_0000335019"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 119..121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 194..199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 104
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ SEQUENCE 432 AA; 47267 MW; 7FF007D754BF1F56 CRC64;
MQLLTIGINH HTAPVALRER VAFPLEQIKP ALSTFKSVFL GHPAPNAPEA AILSTCNRTE
LYCATDDRAA RDAAIRWMSD YHRIPADELA PHVYALPQSE AVRHAFRVAS GLDSMVLGET
QILGQMKNAV RTASEAGSLG TYLNQLFQRT FAVAKEVRGT TEIGAQSVSM AAAAVRLAQR
IFEQVAQQRV LFIGAGEMIE LCATHFAAQG PRELVVANRT AERGAKLAER FGGRAMPLSD
LPARMHEFDI IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV
FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDARSIVPVI RHMHTQADAL
RRAELERARK MLARGDDPAA VLDALSQALT NKLIHGPTSA LNRANGADRD SLIDLMRGFY
QHAPRSSDTS DH
