ID   HEM1_ALCBS              Reviewed;         418 AA.
AC   Q0VS78;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   04-NOV-2008, entry version 26.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=ABO_0522;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15970.1; -; Genomic_DNA.
DR   RefSeq; YP_692242.1; -.
DR   GeneID; 4212665; -.
DR   GenomeReviews; AM286690_GR; ABO_0522.
DR   KEGG; abo:ABO_0522; -.
DR   NMPDR; fig|393595.12.peg.518; -.
DR   HOGENOM; Q0VS78; -.
DR   BioCyc; ABOR393595:ABO_0522-MON; -.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:HAMAP.
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.
DR   InterPro; IPR006151; Shikm_DHase/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   PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 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    418       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000004590.
FT   NP_BIND     186    191       NADP (By similarity).
FT   REGION       49     52       Substrate binding (By similarity).
FT   REGION      111    113       Substrate binding (By similarity).
FT   ACT_SITE     50     50       Nucleophile (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   SITE         96     96       Important for activity (By similarity).
SQ   SEQUENCE   418 AA;  46630 MW;  09415E69BADCE528 CRC64;
     MNLVAVGVNH TTADVELRER LAFSTQQAEV ALASLREMPG VREAALLSTC NRTELYCLTD
     DVTPNFAQWL ASSRNLSVER LSTVLYQHTG EQALEHMMRV AGGLDSLVLG EPQILGQMRE
     AYARAHEAGL LNGELSRLFQ EVFSVAKRIR TETGIGANPV SVAYAAVSFA RHIFADLKKS
     RALLIGAGEM IELVARHLSE QQVQEITIAN RTQERASELA AAVGGRGISL EELPVALERA
     DILISCTAAP LPIMGKGMVE RALKKRRHRP MFMVDIAVPR DIEPEVGELG DVYLYTVDHL
     QEAIQENVRS RQQAAQEASE LIRDAIVRHR RQRREQDAVK VLRDYREQRK AMAESELEKA
     LQQLRNGGDA EQVLRRFQHS LVNKWLHSPS VTLRKMAADG RAEALLLARE LLLDDDQS
//