ID I4W883_9GAMM Unreviewed; 487 AA.
AC I4W883;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Glutamate synthase, NADH/NADPH small subunit {ECO:0000313|EMBL:EIL95674.1};
GN ORFNames=UU5_10171 {ECO:0000313|EMBL:EIL95674.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL95674.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL95674.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL95674.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIL95674.1}.
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DR EMBL; AJXS01000241; EIL95674.1; -; Genomic_DNA.
DR RefSeq; WP_008212480.1; NZ_AJXS01000241.1.
DR AlphaFoldDB; I4W883; -.
DR PATRIC; fig|1162282.3.peg.1941; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
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; 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; 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.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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 37..70
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53077 MW; EDB1A6B85FC7398E CRC64;
MGKITGFLDH PRQHESSEAP AQRKRHWHEF INHLDDEAAR LQAARCMDCG IPFCHNGCPV
NNVIPDFNDL VYKQDWKRAL DVLQSTNNFP EFTGRICPAP CEAACTLNIS GDAVGIKSIE
HKIIDKGWDE GWVTPQPAAR KTGKKVAVVG SGPAGLAAAQ QLARAGHDVT VFEKNDRAGG
LLRYGIPDFK LEKGHIDRRL EQMRGEGVRF RTGVFVGSAD DAKTSGAAEA VTPAQLQQDF
DAVVIAGGAE TPRDLPVPGR ELDGVHFAMD FLPQQNRVNA GDTLDQQIHA GAKHVVVIGG
GDTGSDCVGT SNRHGAEAVT QFELLPQPPE QENKPLVWPY WPIRLRTSSS HEEGCQRDWS
VATKRFNDDG QGRVKSLTGV RLKWESGKMA EVPGSEFEIR ADLVLLAMGF VSPVQGVLDA
FGVDKDKRGN AKATTDGEGC YRTSVNKVFA AGDMRRGQSL VVWAIREGRQ CARAVDEFLM
GASTLPR
//
