ID   HEM1_ARTS2              Reviewed;         446 AA.
AC   A0JYN2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Arth_2773;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K.,
RA   Nakatsu C.H., Richardson P.;
RT   "Complete sequence of chromosome 1 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-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; CP000454; ABK04152.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_832252.1; -.
DR   GeneID; 4444572; -.
DR   GenomeReviews; CP000454_GR; Arth_2773.
DR   KEGG; art:Arth_2773; -.
DR   TIGR; Arth_2773; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00087; -; 1.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_C.
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   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 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    446       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_0000335010.
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   446 AA;  46394 MW;  E50D8052A049F03E CRC64;
     MVLFSLVATH ADIDLETVAQ LSTGASELAT SALSGSPAVK GAVVLATCNR FEIYGEAPHP
     DDVEAARAAL VAQISERTGL NEQLVSRSFN TRTGGEVSQH LFAVSSGLDS AVVGEREIAG
     QVRRALINAQ HEGTASSGLV RLFQAASKTA KDVGAQTALG SRGLSIVSVA LDLATDLSEN
     PDWSAKKAVV FGTGAYAGAT MSLLRERGCT DISVFSSSGR AEGFVATRGG KALDSDTLPA
     AVAAADVMIG CSGSDTRVEA EELARVRAGS AQTLIAIDLA LTHDFDPAVG ELDGVELLTL
     ESVRLAAPQE QAESLAQASG IVTGAAAAFE QEREARSVDS AIVALRRHTM NVLDAEMEKV
     RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELASNGQ QEQYIAALDA LYGITVEQPA
     AAPAAECPVD HGRAGQAPAD VRRETA
//