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Database: UniProt
Entry: K0V7A1_MYCVA
LinkDB: K0V7A1_MYCVA
Original site: K0V7A1_MYCVA 
ID   K0V7A1_MYCVA            Unreviewed;       488 AA.
AC   K0V7A1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:EJZ10708.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:EJZ10708.1};
GN   Name=gltD {ECO:0000313|EMBL:EJZ10708.1};
GN   ORFNames=MVAC_08314 {ECO:0000313|EMBL:EJZ10708.1};
OS   Mycolicibacterium vaccae ATCC 25954.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ10708.1, ECO:0000313|Proteomes:UP000006072};
RN   [1] {ECO:0000313|EMBL:EJZ10708.1, ECO:0000313|Proteomes:UP000006072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ10708.1,
RC   ECO:0000313|Proteomes:UP000006072};
RX   PubMed=23105074; DOI=10.1128/JB.01462-12;
RA   Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA   Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT   "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL   J. Bacteriol. 194:6339-6340(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:EJZ10708.1}.
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DR   EMBL; ALQA01000013; EJZ10708.1; -; Genomic_DNA.
DR   RefSeq; WP_003931339.1; NZ_JH814693.1.
DR   AlphaFoldDB; K0V7A1; -.
DR   PATRIC; fig|1194972.3.peg.1674; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_1_11; -.
DR   Proteomes; UP000006072; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; 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; 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   ECO:0000313|EMBL:EJZ10708.1}.
FT   DOMAIN          25..132
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          146..459
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   488 AA;  53561 MW;  7F90C29FB8EA3726 CRC64;
     MADPRGFLKF THRETPKRRP VDLRLKDWDE VYEEFSQDTL KEQASRCMDC GIPFCHNGCP
     LGNLIPEWND LVRTNRWRDA IERLHATNNF PEFTGRLCPA PCEGSCVLGI NQDPVTIKQV
     EVEIIDNAFR EGWVVPLPPT KLTGKTVAVV GSGPAGLAAA QQLTRAGHKV TVFERDDRIG
     GLLRYGIPEF KMEKRHIDRR LDQMRAEGTE FRTGVNVGVD ITAAQLRSEF DAVVLAGGAT
     ARRDLPIPGR ELDGIHQAME YLPWANRVQL GDPVIDAEGQ PPITAKGKKV IIIGGGDTGA
     DCLGTSHRQG AVSVHQFEIM PRPPETRADS TPWPTYPLMY RVTSAHEEGG ERVYSVNTEE
     FLGENGRVTG LRGHEVVMKD GKFEKVDGSD FEMEADLVLL AMGFTGPERE GLLTDLQVEM
     SDRGNVGRDD AFATSVPGVY VAGDMGRGQS LIVWAIAEGR AAAAAVDRYL MGNTALPAPI
     KPTAVPQR
//
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