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Database: UniProt
Entry: Q5QZE2_IDILO
LinkDB: Q5QZE2_IDILO
Original site: Q5QZE2_IDILO 
ID   Q5QZE2_IDILO            Unreviewed;       503 AA.
AC   Q5QZE2;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Glutamate synthase, putative {ECO:0000313|EMBL:AAV83410.1};
GN   OrderedLocusNames=IL2578 {ECO:0000313|EMBL:AAV83410.1};
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV83410.1, ECO:0000313|Proteomes:UP000001171};
RN   [1] {ECO:0000313|EMBL:AAV83410.1, ECO:0000313|Proteomes:UP000001171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC   {ECO:0000313|Proteomes:UP000001171};
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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DR   EMBL; AE017340; AAV83410.1; -; Genomic_DNA.
DR   RefSeq; WP_011235801.1; NC_006512.1.
DR   AlphaFoldDB; Q5QZE2; -.
DR   STRING; 283942.IL2578; -.
DR   KEGG; ilo:IL2578; -.
DR   eggNOG; COG0069; Bacteria.
DR   HOGENOM; CLU_026563_1_0_6; -.
DR   OrthoDB; 9795032at2; -.
DR   Proteomes; UP000001171; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR024188; GltB.
DR   InterPro; IPR002932; Glu_synthdom.
DR   PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR   PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..468
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   503 AA;  55723 MW;  D14324B8800CE1EE CRC64;
     MSGNVFSTDS LLTLAQWLAA IFVLAIITLV ISIGVMYVVD KTQNKHTIRH NYPVVGRFRY
     LFERMGEFMR QYFFAMDREE MPFNRAQRSW VYRAAKNADR NVAFGSTRDL SRTGTIIFSN
     APYPPMAEQA TSPEPVIIGP YCQKPYSPVS YFHVSGMSYG ALSPVAVKSL SQGAAKAGCW
     LNTGEGGLSP YHLMGHCDIV FQMGTAKFGV RDKEGRLDED RLAELGRHDN VKMFEIKLSQ
     GAKPGKGGIL PGIKVNKEIA QIRGLVEGED AISPNRHPEI SNNEELLDFI EKVRKITGKP
     TGFKFVMGDP SWIDELVDCI LTRGEEYAPD FITLDSADGG TGAAPQPLMD YVGLRVTESL
     PMLIDKLTEA GLHGRIRVVV SGKMITPADV AWAIAMGVDF VTSARGFMFS LGCIQAMQCN
     KNTCPTGVTT DDPKLMRGLD PEDKSVRVAN YHKYMEYGVN IIAHSCGVTD PRRLNRRHAR
     VIKPDGESIS LAERYPLPPA RRR
//
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