ID Q9KPJ3_VIBCH Unreviewed; 489 AA.
AC Q9KPJ3;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Glutamate synthase, small subunit {ECO:0000313|EMBL:AAF95517.1};
GN OrderedLocusNames=VC_2374 {ECO:0000313|EMBL:AAF95517.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF95517.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF95517.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; AE003852; AAF95517.1; -; Genomic_DNA.
DR PIR; F82085; F82085.
DR RefSeq; NP_232004.1; NC_002505.1.
DR RefSeq; WP_000513713.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KPJ3; -.
DR STRING; 243277.VC_2374; -.
DR DNASU; 2613043; -.
DR EnsemblBacteria; AAF95517; AAF95517; VC_2374.
DR KEGG; vch:VC_2374; -.
DR PATRIC; fig|243277.26.peg.2261; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_6; -.
DR Proteomes; UP000000584; Chromosome 1.
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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584}.
FT DOMAIN 38..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 489 AA; 53431 MW; D86D49FD8DD9D37E CRC64;
MGKATGFLEF GRELPKKIDP AERIKNNKEF VLNQEFGKKI NQQASRCMDC GVPFCHNGCP
IGNIIPEFND AVYRDSWEEA WNILSSTNNF PEFTGRVCPA PCETACVLGI NQDPITICNI
EKTIVERAYQ EGYAKPKTPR SRTGKTVAII GSGPAGLAAA EQLNAAGHSV TVFERDEKVG
GLLRFGIPDF KLGMDVIDRK INLMEQAGVK FVVNAHIGVD INAQQLRQEF DAVLLTGGST
VPRDLSIPGR DLKGVYFAMQ FLAQNNRRAN GMDLKGEEIH AKGKHVVVIG GGDTGSDCVG
TSNRHGAASI TQVEIMPIPP QKRPVNMPWP QYPMILRTST SHEEGCERHW NILTKEFIGN
EQGEVTGLRI ADIVWKDAAP GERPSFDEVV GSERVIPCDM AFLAMGFLHP EPHGVLAQLG
IKLDERGNVA TQDFATNQKG VFAAGDMRTG QSLVVRCINE GRECARAVDT FLMGNTHLEA
KADSLMLSA
//
