ID HEM1_METFK Reviewed; 414 AA.
AC Q1GYE9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Glutamyl-tRNA reductase;
DE Short=GluTR;
DE EC=1.2.1.70;
GN Name=hemA; OrderedLocusNames=Mfla_2473;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E.,
RA Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I.,
RA Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) 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; CP000284; ABE50738.1; -; Genomic_DNA.
DR RefSeq; YP_546579.1; NC_007947.1.
DR ProteinModelPortal; Q1GYE9; -.
DR STRING; 265072.Mfla_2473; -.
DR EnsemblBacteria; ABE50738; ABE50738; Mfla_2473.
DR GeneID; 4001569; -.
DR KEGG; mfa:Mfla_2473; -.
DR PATRIC; 32270769; VBIMetFla97085_2593.
DR eggNOG; COG0373; -.
DR HOGENOM; HOG000109650; -.
DR KO; K02492; -.
DR OMA; GPILNRL; -.
DR ProtClustDB; CLSK2529815; -.
DR BioCyc; MFLA265072:GHWJ-2534-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 1 414 Glutamyl-tRNA reductase.
FT /FTId=PRO_1000004638.
FT NP_BIND 184 189 NADP (By similarity).
FT REGION 48 51 Substrate binding (By similarity).
FT REGION 109 111 Substrate binding (By similarity).
FT ACT_SITE 49 49 Nucleophile (By similarity).
FT BINDING 104 104 Substrate (By similarity).
FT BINDING 115 115 Substrate (By similarity).
FT SITE 94 94 Important for activity (By similarity).
SQ SEQUENCE 414 AA; 45810 MW; 0C8AF430F0F13B0C CRC64;
MHLFTVGVNH TTAPVSIREN VAFQNEHLSG ALRDLNSHGI REAAILSTCN RTELYCNTDD
PQKALEWLAN YHRLKPQAIA PYMYTLPQEN AVKHAFRVAS GLDSMVLGEA QILGQMKQAV
RIAENAGTLG TLLHKLFQRT FSVAKEVRTN TNIGANSVSL AAASTRLAQR IFGALNNQHV
LFIGAGEMIE LCAEHFAAHR PLSLTVANRT LERGQELAAS IGGTSMLLAD LPDRLAEFDI
VITSTASQLP IVGLGMVERA IRARKHKPMF MVDLAVPRDI EPEAGELDDV FLYTVDDLAQ
IVQEGMENRQ EAAAEAEAII DMRVENFMQW LKTRSAVPTI RALREQAERH RLNELEKARK
LLARGHDPAQ VLDALSNALT NKLLHGPSHA LNSATGEDRE QLEATLRQLY QIHH
//
