HEM1_KOCRD
ID HEM1_KOCRD Reviewed; 437 AA.
AC B2GL19;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=KRH_08480;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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}.
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DR EMBL; AP009152; BAG29195.1; -; Genomic_DNA.
DR RefSeq; WP_012397916.1; NC_010617.1.
DR AlphaFoldDB; B2GL19; -.
DR SMR; B2GL19; -.
DR STRING; 378753.KRH_08480; -.
DR PRIDE; B2GL19; -.
DR EnsemblBacteria; BAG29195; BAG29195; KRH_08480.
DR KEGG; krh:KRH_08480; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_4_1_11; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 1358620at2; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000008838; 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 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 PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..437
FT /note="Glutamyl-tRNA reductase"
FT /id="PRO_1000190532"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 47
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 46..49
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 116..118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT BINDING 192..197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT SITE 101
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ SEQUENCE 437 AA; 46442 MW; 5C9A0BA85B99378A CRC64;
MVLFCLVASH RTVDLNTVAR LSTGALGVAE DAVSRGALAG AITLSTCNRL ELYGELPEHA
SVDVPGAQQQ LAERIARRAG LDERFVLETM DAYEGPEVPR HLFTVVSGLE SAVVGEREIT
GQVRRALAGA QQSGTASPHL VQLFEAAART AREVGASTGL GERGRSIVSV ALDLADDITS
GDWPERHALV FGTGAYAGAT MAALRDRGCA DIEVYSGSGR AQQFTDQRGG SPVTDESLPG
ALRRADVIIG CSGGSAPMPA SRFPAGPRTV VDLALARDFD PAVADLPNVE LITLESVRVA
APEETRESVA AAREIVERAA RDFENARTAR SMDQAIVALR KHTMAVLDAE LDKVRTHHGC
TGAEEQIEMA MRRMVRSLLH TPTVRARQLA AEGRADEYIT GLEALYGLEV AVPDVPEETA
PSTRQDPSDT PRPRAVG
