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Database: UniProt
Entry: B0VQ37_ACIBS
LinkDB: B0VQ37_ACIBS
Original site: B0VQ37_ACIBS 
ID   B0VQ37_ACIBS            Unreviewed;       473 AA.
AC   B0VQ37;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Glutamate synthase small chain {ECO:0000313|EMBL:CAO99700.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:CAO99700.1};
GN   Name=gltD {ECO:0000313|EMBL:CAO99700.1};
GN   OrderedLocusNames=ABSDF0305 {ECO:0000313|EMBL:CAO99700.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAO99700.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAO99700.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAO99700.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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DR   EMBL; CU468230; CAO99700.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VQ37; -.
DR   KEGG; abm:ABSDF0305; -.
DR   HOGENOM; CLU_000422_3_1_6; -.
DR   OMA; DCVGTAH; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006006; GltD-like.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01318; gltD_gamma_fam; 1.
DR   PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR42783:SF3; 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; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAO99700.1}.
FT   DOMAIN          40..72
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   473 AA;  52172 MW;  63371D45643AE4AD CRC64;
     MAERLNNDFQ FLDVPRQDPE KKDITVRKAE FVEIYKPFTS ETVTNQTHRC LGCGNPYCEW
     KCPVHNYIPN WLKLIAEGQI FQAAELCHQT NTLPEVCGRV CPQDRLCEGA CTLNDGFGAV
     TIGNAEKYIN DTAFALGWRP DMSHVKWTGK KVAIIGAGPA GLGCADILAR GGVKPVVFDK
     RPEIGGLLTF GIPEFKMEKD VMKRRREIFT GMGIEFRLNT EIGKDVTIDE LLAEYDAVFM
     GMGTYTYMKG GFPGEDLDGV YDALDFLISN VNRCQGWEKD PSEYISMDGK KVIVLGGGDT
     AMDCNRTSLR QGAHDVTCAY RRDESNMPGS AREVKNAYEE GVKFLFNRQP IEIVGENGKV
     TGVKVVTTQM GEPDSRGRRS PEPIPGSEEV LPADAVLLAF GFRPSPADWF GSVNINLDGS
     GRVVAPEQQE FKFQTSNPKI FAGGDMVRGS DLVVTAIWEG RQAAEGILDY LGV
//
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