HEM1_CHLP8
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 03-AUG-2022, entry version 138.
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; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; 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 EnsemblBacteria; ACF11155; ACF11155; Cpar_0738.
DR KEGG; cpc:Cpar_0738; -.
DR eggNOG; COG0373; Bacteria.
DR HOGENOM; CLU_035113_2_2_10; -.
DR OMA; FAFKCAA; -.
DR OrthoDB; 1358620at2; -.
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 Gene3D; 3.30.460.30; -; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 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
