ID A0A2K7SP36_9VIBR Unreviewed; 306 AA. AC A0A2K7SP36; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 16-JAN-2019, entry version 6. DE RecName: Full=Glutaminase {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00041476}; DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00041476}; GN Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313}; GN ORFNames=BI375_10855 {ECO:0000313|EMBL:OHY88880.1}; OS Vibrio rotiferianus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=190895 {ECO:0000313|EMBL:OHY88880.1, ECO:0000313|Proteomes:UP000180133}; RN [1] {ECO:0000313|EMBL:OHY88880.1, ECO:0000313|Proteomes:UP000180133} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HM-10 {ECO:0000313|EMBL:OHY88880.1, RC ECO:0000313|Proteomes:UP000180133}; RA Yang Q.; RT "Isolation, identification and antibiotic sensitivity analysis of RT bacterial pathogen from juvenile Hippocampus erectus with tail-rotted RT disease."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00313, CC ECO:0000256|SAAS:SAAS01120526}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00313, CC ECO:0000256|SAAS:SAAS00559507}. CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000256|HAMAP- CC Rule:MF_00313, ECO:0000256|SAAS:SAAS00551679}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OHY88880.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MKFT01000060; OHY88880.1; -; Genomic_DNA. DR RefSeq; WP_005425799.1; NZ_KV861319.1. DR SMR; A0A2K7SP36; -. DR GeneID; 5554071; -. DR KEGG; vro:BSZ04_10365; -. DR KO; K01425; -. DR Proteomes; UP000180133; Unassembled WGS sequence. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro. DR HAMAP; MF_00313; Glutaminase; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR015868; Glutaminase. DR PANTHER; PTHR12544; PTHR12544; 1. DR Pfam; PF04960; Glutaminase; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR TIGRFAMs; TIGR03814; Gln_ase; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_00313}; KW Complete proteome {ECO:0000313|Proteomes:UP000180133}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313, KW ECO:0000256|SAAS:SAAS00041473}. FT BINDING 64 64 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 115 115 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 159 159 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 190 190 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 242 242 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00313}. FT BINDING 260 260 Substrate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00313}. SQ SEQUENCE 306 AA; 32846 MW; 5FFCB7CDFD05DE03 CRC64; MKPTAQILTD ILAEVRPLIG QGKVADYIPA LAKVPNTKLG IAVYTNEGEV IKAGDAEESF SIQSISKALS LTLAMCLYKQ EEIWCRVGKE PSGQAFNSMI QLEMEQGIPR NPFINAGAIV VADLLQSRLS APRQRLLEFA RQLSGDTHIV YDKVVAASEM MHGDRNAAIA YLMRSFGNFE NEVIPVLQNY FHACALKMSC VDLAKTFSYL ANKGTSVQTG KPVVSPTQTK QLNALLATCG LYDGAGEFAY RVGMPGKSGV GGGIIAVVPG EMTIAVWSPE LDASGNSLAG TKALELLAER IGRSIF //