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Database: UniProt
Entry: A0A2T4IGW5_9RHOO
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Original site: A0A2T4IGW5_9RHOO 
ID   A0A2T4IGW5_9RHOO        Unreviewed;       374 AA.
AC   A0A2T4IGW5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=C8261_06010 {ECO:0000313|EMBL:PTD96956.1};
OS   Pseudothauera lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Pseudothauera.
OX   NCBI_TaxID=2136175 {ECO:0000313|EMBL:PTD96956.1, ECO:0000313|Proteomes:UP000241193};
RN   [1] {ECO:0000313|EMBL:PTD96956.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD96956.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PTD96956.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD96956.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Liang Q.-Y.;
RT   "Thauera lacus sp. nov., isolated from an saline lake in Inner Mongolia,
RT   China.";
RL   Submitted (APR-2018) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00456}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PTD96956.1}.
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DR   EMBL; PZKC01000004; PTD96956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4IGW5; -.
DR   OrthoDB; 9804434at2; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000241193; 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; 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: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:UP000241193};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00456}.
FT   DOMAIN          281..363
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         173..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   374 AA;  39969 MW;  3FB623E12D4B876E CRC64;
     MRTKIRDARR LVVKVGSTLV TNNGTGLDKQ AMADWARQIA ALRAGGRKIA LVSSGAIAAG
     MQRLGWSKRP HEMHRLQAAA AVGQMGLVEA YEEAFARHGL HTAQILLTHE DLADRKRYLN
     ARSTLNTLLD LGVVPIINEN DTIVTDEIKF GDNDTLGALV ANLIEADALI ILTDQKGLYT
     ADPRRDPAAE LISEGQAEDR RFEAMAGGAG SGISKGGMIT KVRAAQRAAR SGAHTCIASG
     HESDALTRLG DGEQLGTLLY ASSTPLQARK QWLADHLQLA GSLILDEGAA AALHAGRSLL
     AVGVIEVRGE FERGAAVSLH DASGQELGRG LINYNSAEAR RIARQPSSRI EAILGYIDEP
     ELIHRDHMVV RAAG
//
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