ID HEM1_ARTCA Reviewed; 441 AA.
AC B8HBS2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=Achl_2495;
OS Arthrobacter chlorophenolicus (strain A6 / ATCC 700700 / DSM 12829 /
OS JCM 12360).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micrococcineae; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A6 / ATCC 700700 / DSM 12829 / JCM 12360;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus
RT A6.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CC -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure
CC with each monomer consisting of three distinct domains arranged
CC along a curved 'spinal' alpha-helix. The N-terminal catalytic
CC domain specifically recognizes the glutamate moiety of the
CC substrate. The second domain is the NADPH-binding domain, and the
CC third C-terminal domain is responsible for dimerization (By
CC similarity).
CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC nucleophile attacking the alpha-carbonyl group of tRNA-bound
CC glutamate with the formation of a thioester intermediate between
CC enzyme and glutamate, and the concomitant release of tRNA(Glu).
CC The thioester intermediate is finally reduced by direct hydride
CC transfer from NADPH, to form the product GSA (By similarity).
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
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DR EMBL; CP001341; ACL40460.1; -; Genomic_DNA.
DR RefSeq; YP_002488549.1; NC_011886.1.
DR ProteinModelPortal; B8HBS2; -.
DR STRING; 452863.Achl_2495; -.
DR EnsemblBacteria; ACL40460; ACL40460; Achl_2495.
DR GeneID; 7293970; -.
DR KEGG; ach:Achl_2495; -.
DR PATRIC; 20991627; VBIArtChl38304_3182.
DR eggNOG; COG0373; -.
DR HOGENOM; HOG000109649; -.
DR KO; K02492; -.
DR OMA; EDIMIEL; -.
DR ProtClustDB; PRK00045; -.
DR BioCyc; ACHL452863:GH1A-2547-MONOMER; -.
DR UniPathway; UPA00251; UER00316.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:HAMAP.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR018214; Pyrrol_synth_GluRdtase_CS.
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; SSF69075; 4pyrrol_synth_GluRdtase_C; 1.
DR SUPFAM; SSF69742; GlutR; 1.
DR TIGRFAMs; TIGR01035; hemA; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 3: Inferred from homology;
KW Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1 441 Glutamyl-tRNA reductase.
FT /FTId=PRO_1000118465.
FT NP_BIND 192 197 NADP (By similarity).
FT REGION 47 50 Substrate binding (By similarity).
FT REGION 115 117 Substrate binding (By similarity).
FT ACT_SITE 48 48 Nucleophile (By similarity).
FT BINDING 110 110 Substrate (By similarity).
FT BINDING 121 121 Substrate (By similarity).
FT SITE 100 100 Important for activity (By similarity).
SQ SEQUENCE 441 AA; 45570 MW; D7D32001BF5E225D CRC64;
MVLFSLVATH ADIDLETVAQ LSNGSSGIAA SVLSGSPAVS GAVVLATCNR YEIYGEAPNT
DDVEAARAAL VAQISAQSGL AEPLVSRSFS TRTGPEVTRH LFAVSAGLDS AVVGEREIAG
QVRRALITAQ HEGTASSGLV RLFQAASKTA KDVGAQTALG SRGLSIVSVA LDLATDLSEN
PDWSAKKVVV FGTGAYAGAT MALLRERGCT DVSVFSSSGR AEGFVATRGG TALDADSLRP
AVAAADVMIG CSGSDTRVEA DELAQVRAGS AQPLIAIDLA LTHDFDPAVG ELNGVELLTL
ESVRLAAPQE QAESLAQASG IVKGAAKAFE QEREARSVDS AIVALRRHTM DVLDAEMEKV
RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELAANGQ QDDYVAALEA LYGITVEQPG
TAAPAAGQAE CPVDHKGLES A
//
