ID Q92AS5_LISIN Unreviewed; 489 AA.
AC Q92AS5;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Lin1844 protein {ECO:0000313|EMBL:CAC97075.1};
GN OrderedLocusNames=lin1844 {ECO:0000313|EMBL:CAC97075.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC97075.1, ECO:0000313|Proteomes:UP000002513};
RN [1] {ECO:0000313|EMBL:CAC97075.1, ECO:0000313|Proteomes:UP000002513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; AL596170; CAC97075.1; -; Genomic_DNA.
DR PIR; AC1663; AC1663.
DR RefSeq; WP_010990985.1; NC_003212.1.
DR AlphaFoldDB; Q92AS5; -.
DR STRING; 272626.gene:17566200; -.
DR DNASU; 1130521; -.
DR KEGG; lin:lin1844; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002513; Chromosome.
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 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..140
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 154..471
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53260 MW; 16AC5D7858AD66F6 CRC64;
MGKATGFMEY DRIPSPGRDP KSRTRDWNEY SLPMPVADLT LQAARCMDCG VPFCSVGMEI
KNGVSGCPLH NLIPEWNDAV YRGDWYEALQ LLLKTNNFPE FTGRICPAPC EGGCTVAISE
PAVGIKSIEK AIIDRGFEEG WIKPQPPKKR TGKRIAVIGS GPAGLACADQ LNKAGHSVTV
IEKSDRIGGL LMYGIPTMKL EKEQVTRRVN LMAEEGIEFV TGVAAGTDVT FAELRAEYDS
IVLATGAGNA RDIPLAGRDA AGIHFAVPYL TQSTRDNLDN GGVQTLSAKD KNVVIIGGGD
TGADCVATAL RQGAKSIYQF GIQDKLPELR NGENPWPQYP RVFKMDYAHE EAEAVYGRDP
REYLINTTSF EKDAAGNLVG LHTVEVTEDK ETRQYTPVEG SEKYFEVDMV LIAIGFSGTT
EDIFTNFGVG KTERHTIDAA KGFYRTSEEG VFACGDARHG QSLVVTAIAE GREAAREVDF
YLMGETFLP
//