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Database: UniProt
Entry: B8HBS2
LinkDB: B8HBS2
Original site: B8HBS2 
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-OCT-2014, entry version 45.
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};
GN   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). {ECO:0000255|HAMAP-
CC       Rule:MF_00087}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000255|HAMAP-
CC       Rule:MF_00087}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       1/2. {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
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00087}.
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. {ECO:0000255|HAMAP-
CC       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; 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; PYLYVHY; -.
DR   OrthoDB; EOG6MWNBM; -.
DR   BioCyc; ACHL452863:GH1A-2547-MONOMER; -.
DR   UniPathway; UPA00251; UER00316.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; IPR018214; GluRdtase_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; SSF69075; 1.
DR   SUPFAM; SSF69742; SSF69742; 1.
DR   TIGRFAMs; TIGR01035; hemA; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    441       Glutamyl-tRNA reductase.
FT                                /FTId=PRO_1000118465.
FT   NP_BIND     192    197       NADP. {ECO:0000255|HAMAP-Rule:MF_00087}.
FT   REGION       47     50       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   REGION      115    117       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   ACT_SITE     48     48       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   BINDING     110    110       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   BINDING     121    121       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00087}.
FT   SITE        100    100       Important for activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00087}.
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
//
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