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Database: UniProt
Entry: K9ALQ6_9STAP
LinkDB: K9ALQ6_9STAP
Original site: K9ALQ6_9STAP 
ID   K9ALQ6_9STAP            Unreviewed;       485 AA.
AC   K9ALQ6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:EKU48239.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:EKU48239.1};
GN   Name=gltD {ECO:0000313|EMBL:EKU48239.1};
GN   ORFNames=C273_06017 {ECO:0000313|EMBL:EKU48239.1};
OS   Staphylococcus massiliensis S46.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU48239.1, ECO:0000313|Proteomes:UP000009885};
RN   [1] {ECO:0000313|EMBL:EKU48239.1, ECO:0000313|Proteomes:UP000009885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S46 {ECO:0000313|EMBL:EKU48239.1,
RC   ECO:0000313|Proteomes:UP000009885};
RX   PubMed=23929469;
RA   Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT   "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT   the Surface of Healthy Human Skin.";
RL   Genome Announc. 1:e00553-13(2013).
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:EKU48239.1}.
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DR   EMBL; AMSQ01000007; EKU48239.1; -; Genomic_DNA.
DR   RefSeq; WP_009383378.1; NZ_AMSQ01000007.1.
DR   AlphaFoldDB; K9ALQ6; -.
DR   STRING; 1229783.C273_06017; -.
DR   PATRIC; fig|1229783.3.peg.1218; -.
DR   eggNOG; COG0493; Bacteria.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000009885; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EKU48239.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009885}.
FT   DOMAIN          28..140
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          154..468
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   485 AA;  54413 MW;  E2DAF8399AC1FFA2 CRC64;
     MGEFKGFMKY DKASLPELSL VERLKHHGAF QQAFDKADAS IQAARCMDCG TPFCQTGIGV
     EKDTIGCPIG NYIPEWNDLV YLEDYEAAYY RLSETNNFPD FTGRVCPAPC ESSCVMAINR
     ESVAIKGIER TIIDEAFEQG WVQPRRPERR LNEKIAIIGS GPCGLTAADE LNALGYDVTV
     IERAPSPGGL LMYGIPNMKL DKHVVERRVE LMEEAGVTFK LNTEVGKDIM KETLLATYDA
     VILCTGAEKP RDLPLEGRMS PDIHFAMDYL TEQTLLERGE IEQATITAKD KRVIVIGAGD
     TGADCVATAL REGCHSVVQF NKYDRLPDDV DENVSWPRPK EVFKMDYAHR EYEAKYGLEP
     RAYGVQTMRY DVDRIGRLKG VYTQLVNDEQ HDLDMSLAPE RFWPADLVLL SIGFIGTNQH
     VPEHFRVKLS QNKIKADDKN YQTNVKNVFA AGDARRGQSL VVWAIKEGRG VAKSVHHYLQ
     SKVLS
//
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