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Database: UniProt
Entry: B4VVG2_9CYAN
LinkDB: B4VVG2_9CYAN
Original site: B4VVG2_9CYAN 
ID   B4VVG2_9CYAN            Unreviewed;       438 AA.
AC   B4VVG2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
DE            Short=GluTR {ECO:0000256|HAMAP-Rule:MF_00087};
DE            EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|HAMAP-Rule:MF_00087};
GN   Name=hemA {ECO:0000256|HAMAP-Rule:MF_00087};
GN   ORFNames=MC7420_4195 {ECO:0000313|EMBL:EDX74210.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX74210.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX74210.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX74210.1,
RC   ECO:0000313|Proteomes:UP000003835};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC         glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC         COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78520; EC=1.2.1.70;
CC         Evidence={ECO:0000256|ARBA:ARBA00001415, ECO:0000256|HAMAP-
CC         Rule:MF_00087, ECO:0000256|RuleBase:RU000584};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005059, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure with
CC       each monomer consisting of three distinct domains arranged along a
CC       curved 'spinal' alpha-helix. The N-terminal catalytic domain
CC       specifically recognizes the glutamate moiety of the substrate. The
CC       second domain is the NADPH-binding domain, and the third C-terminal
CC       domain is responsible for dimerization. {ECO:0000256|HAMAP-
CC       Rule:MF_00087}.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC       with the formation of a thioester intermediate between enzyme and
CC       glutamate, and the concomitant release of tRNA(Glu). The thioester
CC       intermediate is finally reduced by direct hydride transfer from NADPH,
CC       to form the product GSA. {ECO:0000256|HAMAP-Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|HAMAP-Rule:MF_00087,
CC       ECO:0000256|RuleBase:RU000584}.
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DR   EMBL; DS989854; EDX74210.1; -; Genomic_DNA.
DR   RefSeq; WP_006102515.1; NZ_DS989854.1.
DR   AlphaFoldDB; B4VVG2; -.
DR   STRING; 118168.MC7420_4195; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_2_2_3; -.
DR   OrthoDB; 110209at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   Gene3D; 3.30.460.30; Glutamyl-tRNA reductase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036453; GluRdtase_dimer_dom_sf.
DR   InterPro; IPR036343; GluRdtase_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   NCBIfam; TIGR01035; hemA; 1.
DR   PANTHER; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF1; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 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   SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR   SUPFAM; SSF69075; Glutamyl tRNA-reductase dimerization domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00747; GLUTR; 1.
PE   3: Inferred from homology;
KW   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00087};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00087};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00087}; Reference proteome {ECO:0000313|Proteomes:UP000003835}.
FT   DOMAIN          6..156
FT                   /note="Glutamyl-tRNA reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05201"
FT   DOMAIN          171..307
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          321..421
FT                   /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00745"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-1"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         114..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-2"
FT   BINDING         189..194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-3"
FT   SITE            99
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00087,
FT                   ECO:0000256|PIRSR:PIRSR000445-4"
SQ   SEQUENCE   438 AA;  49027 MW;  145401626B01F605 CRC64;
     MNLAVVGLSY KTTPVEIREK LSISEAKREQ AIAHLCTYPH IEEVAILNTC NRLEIYMVVL
     ETDQAIREVT EFLAQQGQLP FHQLYQHLFI LRQQDVLRHL MQVASGLDSL VLGEGQILAQ
     VKHTYKLCQQ YNGIKCILNQ LFKHAITAAK RVRNETKIGT GAVSISSAAV ELAQLKVANL
     STCQVTIVGA GKMARRLVQH LLAKGVKQIS IVNRSLEGAK VFANQFSDAN LSCYSLAEMM
     SVIAKSHIVF TSTAATETLV NRAKLATVLA PNQPLMLFDI SVPRNVDADV NQLDHIQVFN
     VDDLQTVVTQ NQDYRQQMAI EAQRLIEAEV EAFSAWWRSR ETVSTISCLR KKAETIREQE
     LEKALSRLGS EFGKKHQEVI EALTRGIVNK LLHEPMVQLR TQPDLEAQRL AISTLQVLFN
     LEPGNSNYTS VTKVPYSQ
//
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