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Database: UniProt
Entry: Q2L1U1_BORA1
LinkDB: Q2L1U1_BORA1
Original site: Q2L1U1_BORA1 
ID   Q2L1U1_BORA1            Unreviewed;       647 AA.
AC   Q2L1U1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   OrderedLocusNames=BAV0087 {ECO:0000313|EMBL:CAJ47689.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ47689.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ47689.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ47689.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001031};
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DR   EMBL; AM167904; CAJ47689.1; -; Genomic_DNA.
DR   RefSeq; WP_012415791.1; NC_010645.1.
DR   AlphaFoldDB; Q2L1U1; -.
DR   STRING; 360910.BAV0087; -.
DR   GeneID; 41392017; -.
DR   KEGG; bav:BAV0087; -.
DR   eggNOG; COG0037; Bacteria.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_404236_0_0_4; -.
DR   OMA; PLFMAGD; -.
DR   OrthoDB; 8557965at2; -.
DR   Proteomes; UP000001977; Chromosome.
DR   CDD; cd00352; Gn_AT_II; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..243
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   647 AA;  72674 MW;  BA74BB75A079B42C CRC64;
     MCGIFGLVVA RQSTLKTDDI SKLLKRLFLL SESRGKEAAG LAAAAGQTLR VLKYPVPASE
     LLKMQEYKRQ VEQAVSQRDQ TGLGIVGHAR LVTNGQQGVD ANNQPVVRDS VVVVHNGIIV
     NEAEIWAAEP RLKKLAQVDT EVVAALMNDR LARGAPIEQV CREVFGKIYG EASLGVLFAD
     RDDLLLATNT GSLNYLHAPK QGVFVFVSEY VIAKRIREEM KEHIEFGDPQ PVRAGQAMTI
     RIESAQPGPL FSLGLPYSPA ETAAPILAAP APVLRKVVSN VEEQQRRYAG LRRCSKCVLP
     ETMPFIEFDE QGVCNYCNNY KPAKLKGRKE LDKLLEKYRS NNGSADCLVG FSGGRDSSYG
     LHLLKTELGM NPIAYTYDWG MVTDLARRNQ ARLCGKLGVE HIWVSADIKQ KRANVGVNVN
     AWLKNPDLGM IPLFMAGDKQ FMYHANRLMK ETGIKLMVYS TNHLERTDFK VGFCGVRPAS
     AGVQLNKVSS MQKAQLALYY MKNYLVNPGY INQSLLDTFT AFLSYYFVNQ DFLYLFDYLE
     WDEATINKVL IETYDWELAP DTPTTWRIGD GTAPFYNYIY QTVAGFTEYE TFRSNQIREG
     VITREEAFML IEKENIARID AIQDYCRLIG VDFDKAMRVI NSIPKLY
//
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