ID A0A0F7HCC9_SERFO Unreviewed; 367 AA.
AC A0A0F7HCC9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 ECO:0000313|EMBL:MBC3253454.1};
GN ORFNames=BSQ40_15320 {ECO:0000313|EMBL:OKP27279.1}, CRN79_04635
GN {ECO:0000313|EMBL:ATM75174.1}, H8I91_24625
GN {ECO:0000313|EMBL:MBC3253454.1}, NCTC12965_01725
GN {ECO:0000313|EMBL:VTR23242.1}, NCTC13193_01200
GN {ECO:0000313|EMBL:VEI64608.1}, WN53_13630
GN {ECO:0000313|EMBL:AKG70054.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG70054.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG70054.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG70054.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OKP27279.1, ECO:0000313|Proteomes:UP000186436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5l {ECO:0000313|EMBL:OKP27279.1,
RC ECO:0000313|Proteomes:UP000186436};
RA Goncharov A., Grigoriev S., Azarov D., Kolodzhieva V., Tikhonov A.,
RA Akhremenko Y., Tarasova L., Zueva L., Suvorov A.;
RT "Draft genome sequence of Serratia fonticola 5l isolated from intestinal
RT tract content of a 9000-year-old elk (Alces alces) from permafrost on the
RT Omoloy river.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATM75174.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM75174.1};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ATM75174.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_411 {ECO:0000313|EMBL:ATM75174.1};
RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Ott S., Zhao X.,
RA Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S., Geyer C.,
RA Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:VTR23242.1, ECO:0000313|Proteomes:UP000358076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12965 {ECO:0000313|EMBL:VTR23242.1,
RC ECO:0000313|Proteomes:UP000358076}, and NCTC13193
RC {ECO:0000313|EMBL:VEI64608.1, ECO:0000313|Proteomes:UP000270487};
RG Pathogen Informatics;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:MBC3253454.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UPMP2131 {ECO:0000313|EMBL:MBC3253454.1};
RA Richter L., Du Plessis E.M., Duvenage S., Allam M., Korsten L.;
RT "Food and environmental bacterial isolates.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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; CP011254; AKG70054.1; -; Genomic_DNA.
DR EMBL; CP023956; ATM75174.1; -; Genomic_DNA.
DR EMBL; JACNYM010000031; MBC3253454.1; -; Genomic_DNA.
DR EMBL; MQRH01000013; OKP27279.1; -; Genomic_DNA.
DR EMBL; LR134492; VEI64608.1; -; Genomic_DNA.
DR EMBL; CABEEZ010000031; VTR23242.1; -; Genomic_DNA.
DR RefSeq; WP_024483654.1; NZ_SUPV01000016.1.
DR AlphaFoldDB; A0A0F7HCC9; -.
DR STRING; 47917.AV650_09185; -.
DR GeneID; 30321209; -.
DR KEGG; sfw:WN53_13630; -.
DR PATRIC; fig|47917.8.peg.2816; -.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000034699; Chromosome.
DR Proteomes; UP000186436; Unassembled WGS sequence.
DR Proteomes; UP000221800; Chromosome.
DR Proteomes; UP000270487; Chromosome 1.
DR Proteomes; UP000358076; Unassembled WGS sequence.
DR Proteomes; UP000596701; Unassembled WGS sequence.
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; 1.
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:SF1; ISOPENTENYL PHOSPHATE 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:UP000034699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00456}.
FT DOMAIN 276..359
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT BINDING 10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 169..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 211..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 367 AA; 39126 MW; ED785D1413F9F438 CRC64;
MNGSQTLVVK LGTSVLTGGS LRLNRAHIVE LVRQCAQQHA AGHRIVIVTS GAIAAGREHL
GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHIGQ MLLTRADLED RERFLNARDT
MTALLDNRIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QQGLYTADPR
NNPEAELIRE VHGVDDALRA IAGDSVSGLG TGGMGTKLQA ADVACRAGID VIIAAGSKPG
VVADVIEGNP VGTRFHALET PLENRKRWIF GAPPAGEITV DDGAVEAMMA RGSSLLPKGI
RDVKGDFSRG EVIRIRNLAG RDLAHGVSRY NSDAMRMIAG HHSQQISEIL GYEYGPVAVH
RDDMIVS
//
