ID A0A0T7C0N3_9CYAN Unreviewed; 369 AA.
AC A0A0T7C0N3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glutamate 5-kinase {ECO:0000256|HAMAP-Rule:MF_00456};
DE EC=2.7.2.11 {ECO:0000256|HAMAP-Rule:MF_00456};
DE AltName: Full=Gamma-glutamyl kinase {ECO:0000256|HAMAP-Rule:MF_00456};
DE Short=GK {ECO:0000256|HAMAP-Rule:MF_00456};
GN Name=proB {ECO:0000256|HAMAP-Rule:MF_00456};
GN ORFNames=IJ00_25250 {ECO:0000313|EMBL:AKG24837.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG24837.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG24837.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG24837.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to
CC form L-glutamate 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00456};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000256|HAMAP-
CC Rule:MF_00456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00456}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00456}.
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DR EMBL; CP011382; AKG24837.1; -; Genomic_DNA.
DR RefSeq; WP_035159617.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7C0N3; -.
DR STRING; 1337936.IJ00_25250; -.
DR KEGG; calh:IJ00_25250; -.
DR eggNOG; COG0263; Bacteria.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000065745; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04242; AAK_G5K_ProB; 1.
DR CDD; cd21157; PUA_G5K; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 2.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR041739; G5K_ProB.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR NCBIfam; TIGR01027; proB; 1.
DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1.
DR PANTHER; PTHR43654:SF3; GLUTAMATE 5-KINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF000729; GK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00456};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00456};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_00456}; Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00456}.
FT DOMAIN 278..361
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 168..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 212..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 369 AA; 39585 MW; DB08494A4E21E1C8 CRC64;
MAHTIVVKIG TSSLTQPETG QLALSTIATL AETLADLRRQ GHRVILVSSG AVGVGCARLG
LTERPRAIAL KQAVAAVGQG RLMRVYDDLF TTLQQPIAQV LLTRSDLVQR SRYLNIYNTF
QALLELGVIP VVNENDTVAT EELKFGDNDT LSALVASLVQ ADWLFLLTDV DRLYSADPRS
VPDAQPISLV NSLQELTDLQ VQTGTQGSQW GTGGMVTKIA AARIAIAAGV RTVITQGRQP
RNLEKIIGGE TIGTHFAPQP EPTSARKRWI AYGLLPTGKL YLDGGAVQAI ASAGKSLLAA
GITNIEGEFD TQDAVQLCDR DGNEIARGLV NYNSEELQKI RGKRSSDIPL ILGYAGAETV
IHRDNLVLV
//
