ID   HEM12_ANADF             Reviewed;         423 AA.
AC   A7HBF2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Glutamyl-tRNA reductase 2 {ECO:0000255|HAMAP-Rule:MF_00087};
DE            Short=GluTR 2 {ECO:0000255|HAMAP-Rule:MF_00087};
DE            EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087};
GN   Name=hemA2 {ECO:0000255|HAMAP-Rule:MF_00087};
GN   OrderedLocusNames=Anae109_1845;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00087};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC       {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 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:0000255|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:0000255|HAMAP-Rule:MF_00087}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00087}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS26048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000769; ABS26048.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041448240.1; NC_009675.1.
DR   AlphaFoldDB; A7HBF2; -.
DR   SMR; A7HBF2; -.
DR   STRING; 404589.Anae109_1845; -.
DR   KEGG; afw:Anae109_1845; -.
DR   eggNOG; COG0373; Bacteria.
DR   HOGENOM; CLU_035113_2_2_7; -.
DR   OrthoDB; 110209at2; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000006382; 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: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   3: Inferred from homology;
KW   NADP; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..423
FT                   /note="Glutamyl-tRNA reductase 2"
FT                   /id="PRO_0000335008"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         48..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         108..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   BINDING         183..188
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
FT   SITE            93
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00087"
SQ   SEQUENCE   423 AA;  45130 MW;  494272D1FBFC0093 CRC64;
     MLVAVGLNQK GATVADREVL ALPAEGFQST LAEYAALDAV DEIAVMSTCY RVEIYAATRC
     PAAATLSLRQ ALNARAGREL PLFELHGEEA YRHLVRVASS LESAILGEPQ ILGQVKEAFQ
     RSIDQGVAAK ELTSVLNRAL SAAKRVRTDT AIGRAGISWG HAAATLAEKV LGKMQGRRVV
     VVGAGEMARL SAQHLRDQGA RIVVLNRTLV NGEALAREVG GVARPLEALG EELAQADVVV
     SAAPVAPDAF QPEAMAELSR SRKRPIVLVD LAVPRAIPAA TGAIRDVYLC DVDDLDRVMK
     AAMSERAAAV ADADRIIAEE VGKFVRAEAE RRAAPLIQEM RTRASAIARE EVERTLRRLG
     EDPEVERRLE AMAGSIVSKI LHAPSARLRQ AVCDGCSGEA LVSAAVEIFE LSADIRVHRG
     NAA
//