ID   HEM1_CHLP8              Reviewed;         426 AA.
AC   P28462; B3QMK2; O87494;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA; OrderedLocusNames=Cpar_0738;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1793335; DOI=10.1007/bf00262999;
RA   Majumdar D., Avissar Y.J., Wyche J.H., Beale S.I.;
RT   "Structure and expression of the Chlorobium vibrioforme hemA gene.";
RL   Arch. Microbiol. 156:281-289(1991).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS, FUNCTION, HEME BINDING, AND SUBUNIT.
RX   PubMed=15968053; DOI=10.1128/jb.187.13.4444-4450.2005;
RA   Srivastava A., Beale S.I.;
RT   "Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable
RT   homodimer that contains one tightly bound heme per subunit.";
RL   J. Bacteriol. 187:4444-4450(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-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:0000269|PubMed:15968053}.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15968053}.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Was shown to bind heme, but the precise role of heme is
CC       unclear.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000305}.
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DR   EMBL; M96364; AAA23112.1; -; Genomic_DNA.
DR   EMBL; AF080069; AAC61856.1; -; Genomic_DNA.
DR   EMBL; CP001099; ACF11155.1; -; Genomic_DNA.
DR   PIR; A48359; A48359.
DR   RefSeq; WP_012501988.1; NC_011027.1.
DR   AlphaFoldDB; P28462; -.
DR   SMR; P28462; -.
DR   STRING; 517417.Cpar_0738; -.
DR   KEGG; cpc:Cpar_0738; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_2_2_10; -.
DR   OrthoDB; 110209at2; -.
DR   BRENDA; 1.2.1.70; 1348.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000008811; Chromosome.
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-UniRule.
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; PTHR43013; GLUTAMYL-TRNA REDUCTASE; 1.
DR   PANTHER; PTHR43013:SF1; GLUTAMYL-TRNA REDUCTASE; 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   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; NADP; Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN           1..426
FT                   /note="Glutamyl-tRNA reductase"
FT                   /id="PRO_0000114009"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         49..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            99
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        144..145
FT                   /note="TA -> SP (in Ref. 1; AAC61856/AAA23112)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191..223
FT                   /note="GETGELAAKHMYAKNARNIVITNRTQSKAEALA -> VKQSWQQSTCTPRTP
FT                   GTSSSPTGRNPRPRAC (in Ref. 1; AAC61856/AAA23112)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  48142 MW;  D169328D709EF697 CRC64;
     MNIISVGVNH KTAPIEIRER IALSEVQNKE FVTDLVSSGL ASEAMVVSTC NRTELYVVPG
     MPEVNCDYLK DYIISYKDAR NAVRPEHFFN RFYCGTARHL FEVSSAIDSL VLGEGQILGQ
     VKDAYRIAAE VGTAGILLTR LCHTAFSVAK KVKTRTKLME GAVSVSYAAV ELAQKIFSNL
     SMKKVLLIGA GETGELAAKH MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH
     LHEFDIIITA VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD
     IDALKHIIDK NLERRRAELP KVKSIIDEEL IGFGQWINTL KVRPTIVDLQ SKFIEIKEKE
     LERYRHKVSE EELKRMEHLT DRILKKILHH PIKMLKAPVD TADNIPSKVN LVRNIFDLEE
     PNQSLQ
//