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
//