ID Q57A28_BRUAB Unreviewed; 484 AA.
AC Q57A28;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=GltD, glutamate synthase, small subunit {ECO:0000313|EMBL:AAX75506.1};
GN Name=gltD {ECO:0000313|EMBL:AAX75506.1};
GN OrderedLocusNames=BruAb2_0055 {ECO:0000313|EMBL:AAX75506.1};
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX75506.1, ECO:0000313|Proteomes:UP000000540};
RN [1] {ECO:0000313|EMBL:AAX75506.1, ECO:0000313|Proteomes:UP000000540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941 {ECO:0000313|EMBL:AAX75506.1,
RC ECO:0000313|Proteomes:UP000000540};
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; AE017224; AAX75506.1; -; Genomic_DNA.
DR RefSeq; WP_002972210.1; NC_006933.1.
DR AlphaFoldDB; Q57A28; -.
DR EnsemblBacteria; AAX75506; AAX75506; BruAb2_0055.
DR GeneID; 55591792; -.
DR KEGG; bmb:BruAb2_0055; -.
DR HOGENOM; CLU_000422_3_1_5; -.
DR Proteomes; UP000000540; Chromosome II.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 24..131
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 148..465
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 484 AA; 52971 MW; DD7EE3CDFF153DB9 CRC64;
MGKVTGFLEI DRQVAKYQPA SDRIRHFREF TIPMTDGEVQ KQAARCMDCG IPYCHGPTGC
PVHNQIPDWN DLVYNNNWDQ AIRNLHLTNN FPEFTGRICP APCEEACTLN LEDMPVAIKT
VEQALGDKAY ELGYIVPQPA ASKTGKLVAI IGSGPAGLAA AQQLARAGHM VDVYERESRP
GGLLRYGIPD FKMEKHLIDR RVAQMEGEGV RFHCGVNIGV DKPLRGLLDT YDAVLYCGGS
ETPRPAGIPG ADLDGVHDAM PYLVQQNRRV GRENIESVAW ASVPILAGGK HVVVVGGGDT
ASDCVGTAFR QGAVNVTQLD IRPQPPEKED KLSVWPYWAT KMRTSSSQAE GASREFQVAT
LEFIGEDGRL THVKCCQVDE KRRPIAGTEF FIKADLAFIA IGFAGPVEDS VVKEMDGKLE
IATDRRGSKS VKANDRDYRT NVDKLYAAGD IRRGQSLVVW AIREGRQAAH AIDADLMGSS
VLPR
//
