GLNA2_HALMT
ID GLNA2_HALMT Reviewed; 446 AA.
AC I3R584;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Gamma-glutamylputrescine synthetase {ECO:0000305};
DE Short=Gamma-Glu-Put synthetase {ECO:0000305};
DE EC=6.3.1.11 {ECO:0000269|PubMed:34439822};
DE AltName: Full=Glutamate--putrescine ligase {ECO:0000303|PubMed:34439822};
GN Name=glnA2 {ECO:0000303|PubMed:32296946, ECO:0000303|PubMed:34439822};
GN OrderedLocusNames=HFX_1688 {ECO:0000312|EMBL:AFK19394.1};
GN ORFNames=BM92_00670 {ECO:0000312|EMBL:AHZ21256.1},
GN C439_02042 {ECO:0000312|EMBL:EMA04417.1},
GN E6P09_11460 {ECO:0000312|EMBL:QCQ75856.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000312|EMBL:AFK19394.1};
RN [1] {ECO:0000312|EMBL:AFK19394.1, ECO:0000312|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000006469};
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [2] {ECO:0000312|EMBL:EMA04417.1, ECO:0000312|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000011603};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3] {ECO:0000312|EMBL:AHZ21256.1, ECO:0000312|Proteomes:UP000027075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:QCQ75856.1, ECO:0000312|Proteomes:UP000299011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000299011};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000303|PubMed:32296946};
RX PubMed=32296946; DOI=10.1007/s00792-020-01169-x;
RA Rodriguez-Herrero V., Paya G., Bautista V., Vegara A., Cortes-Molina M.,
RA Camacho M., Esclapez J., Bonete M.J.;
RT "Essentiality of the glnA gene in Haloferax mediterranei: gene conversion
RT and transcriptional analysis.";
RL Extremophiles 24:433-446(2020).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND PHYLOGENETIC ANALYSIS.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000303|PubMed:34439822};
RX PubMed=34439822; DOI=10.3390/biom11081156;
RA Rodriguez-Herrero V., Peris A., Camacho M., Bautista V., Esclapez J.,
RA Bonete M.J.;
RT "Novel Glutamate-Putrescine Ligase Activity in Haloferax mediterranei: A
RT New Function for glnA-2 Gene.";
RL Biomolecules 11:0-0(2021).
CC -!- FUNCTION: Involved in the breakdown of putrescine via the biosynthesis
CC of gamma-L-glutamylputrescine. Not required for glutamine synthesis
CC (PubMed:34439822). Is not able to compensate for the loss of glutamine
CC synthetase (PubMed:32296946). {ECO:0000269|PubMed:32296946,
CC ECO:0000269|PubMed:34439822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + putrescine = ADP + gamma-L-
CC glutamylputrescine + H(+) + phosphate; Xref=Rhea:RHEA:13633,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58731, ChEBI:CHEBI:326268,
CC ChEBI:CHEBI:456216; EC=6.3.1.11;
CC Evidence={ECO:0000269|PubMed:34439822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13634;
CC Evidence={ECO:0000269|PubMed:34439822};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P12425};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=3.42 umol/min/mg enzyme (at 42 degrees Celsius in complex medium
CC (CM) in which 40 mM putrescine is both nitrogen and carbon source)
CC {ECO:0000269|PubMed:34439822};
CC Vmax=4.47 umol/min/mg enzyme (at 42 degrees Celsius in defined media
CC (DM) with 40 mM putrescine as the nitrogen source and glucose as the
CC carbon source) {ECO:0000269|PubMed:34439822};
CC Vmax=1.75 umol/min/mg enzyme (at 42 degrees Celsius in defined media
CC (DM) with 40 mM nitrate as the nitrogen source and glucose as the
CC carbon source) {ECO:0000269|PubMed:34439822};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from putrescine. {ECO:0000269|PubMed:34439822}.
CC -!- SUBUNIT: Dodecamer. {ECO:0000269|PubMed:34439822}.
CC -!- INDUCTION: Expression is induced in complex medium (CM) in which
CC putrescine is both nitrogen (N) and carbon (C) source, in defined media
CC (DM) with putrescine as the N source and glucose as the C source, DM
CC with ammonium or nitrate as the N source and glucose as the C source,
CC and in nitrogen starvation media (NS) without the N source and glucose
CC as the C source (at protein level). Not expressed in CM in which yeast
CC extract is both the N and the C source (at protein level).
CC Constitutively expressed at different growth phases in CM in which
CC yeast extract is both the N and the C source and in DM with ammonium or
CC nitrate as the N source and glucose as the C source. Also
CC constitutively expressed in NS regardless of the nitrogen deficiency
CC time (48, 96 or 120 hours). Expression may be regulated at post-
CC transcriptional level (PubMed:34439822). Expression is down-regulated
CC in CM with 40 mM glutamine in the mid-exponential phase after nitrogen
CC starvation for 72 hours (PubMed:32296946).
CC {ECO:0000269|PubMed:32296946, ECO:0000269|PubMed:34439822}.
CC -!- DISRUPTION PHENOTYPE: No glutamate-putrescine ligase activity in
CC complex medium (CM) in which putrescine is both nitrogen (N) and carbon
CC (C) source, in defined media (DM) with putrescine as the N source and
CC glucose as the C source nor in DM with nitrate as the N source and
CC glucose as the C source. {ECO:0000269|PubMed:34439822}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01330, ECO:0000255|PROSITE-
CC ProRule:PRU01331, ECO:0000255|RuleBase:RU000384}.
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DR EMBL; CP001868; AFK19394.1; -; Genomic_DNA.
DR EMBL; AOLO01000002; EMA04417.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ21256.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ75856.1; -; Genomic_DNA.
DR RefSeq; WP_004056714.1; NZ_CP039139.1.
DR SMR; I3R584; -.
DR STRING; 523841.HFX_1688; -.
DR EnsemblBacteria; AFK19394; AFK19394; HFX_1688.
DR EnsemblBacteria; AHZ21256; AHZ21256; BM92_00670.
DR EnsemblBacteria; EMA04417; EMA04417; C439_02042.
DR EnsemblBacteria; QCQ75856; QCQ75856; E6P09_11460.
DR GeneID; 40157043; -.
DR KEGG; hme:HFX_1688; -.
DR PATRIC; fig|523841.21.peg.411; -.
DR eggNOG; arCOG01909; Archaea.
DR HOGENOM; CLU_017290_6_0_2; -.
DR OMA; DWGLDNR; -.
DR OrthoDB; 47310at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF16952; Gln-synt_N_2; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding.
FT CHAIN 1..446
FT /note="Gamma-glutamylputrescine synthetase"
FT /id="PRO_0000454697"
FT DOMAIN 14..105
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 112..446
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 296
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 314
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 337
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ SEQUENCE 446 AA; 49128 MW; 54699B77DF4C1E3E CRC64;
MSDTSTVKSQ CEDQNIDLIR LLYVTPSGVI QANTVDVSEV DAAVESGVTL SEVIQVYDAF
ACRNRNSRFD AVGEVHLCPD PETFRPLPYA DRAGAMLCNI RTLDGEPWDV DSRSSLQSVE
RDLRAKGLSP QVAFESEFSL FSRDGDGKIN RGDEAGAYRT ESIRGTHDAI LHIVDALKAQ
GIDVKKYHPE FSPGKHEIVT GHHTGLEAAD EHLLLRETVK SVAEQDGYQA TFLPKPFDDG
TNGCHINVSL WNGENQFFDP NHGDISETAR QFIAGVLDHA PAVLALTAPT VNSYSRLQPR
HGAAGYICWG WLNREALIRV PAPAQGREAD STRIEFRGAD NTANPYLGLI GLLAAGNDGI
ERELEPPEPV SVDPCDLTDA QRTAKGIKRL PQTLGEALDA LETNEVLREA LGPDLFDAYV
EVKRNHWKLF TESAGAWQRE RLRNLY
