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Database: UniProt
Entry: S3UQW3_9LEPT
LinkDB: S3UQW3_9LEPT
Original site: S3UQW3_9LEPT 
ID   S3UQW3_9LEPT            Unreviewed;       522 AA.
AC   S3UQW3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glutamate synthase domain protein {ECO:0000313|EMBL:EPG72801.1};
GN   ORFNames=LEP1GSC058_0910 {ECO:0000313|EMBL:EPG72801.1};
OS   Leptospira fainei serovar Hurstbridge str. BUT 6.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG72801.1, ECO:0000313|Proteomes:UP000014540};
RN   [1] {ECO:0000313|EMBL:EPG72801.1, ECO:0000313|Proteomes:UP000014540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUT 6 {ECO:0000313|EMBL:EPG72801.1,
RC   ECO:0000313|Proteomes:UP000014540};
RA   Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA   Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA   Sutton G.G., Nelson W.C., Fouts D.E.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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:EPG72801.1}.
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DR   EMBL; AKWZ02000011; EPG72801.1; -; Genomic_DNA.
DR   RefSeq; WP_016551365.1; NZ_AKWZ02000011.1.
DR   AlphaFoldDB; S3UQW3; -.
DR   STRING; 1193011.LEP1GSC058_0910; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000014540; Unassembled WGS sequence.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          156..472
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   522 AA;  58156 MW;  270DCB3D4A13010C CRC64;
     MSEERIFEYL RIIDNHPWLF WSAIVGFLLV AVFIHDIVQR KHTIKHNFPI VGHIRYLFEM
     VGPELRQYWV ANDKEEMPFN RAERSWVYAT AKKQNNNFGF GTTELLYDAG YPIIKHAAFP
     FPEGHAKFVD GDPSMIPSLK VMGEFHRRKK MYRPPSVVNI SAMSYGSLGE RAVSALNQGA
     KLARCYHNTG EGGLSPFHGF GADVMWQLGT GYFGARDEHG RFSMDKFLER LAGNPNVRAI
     EIKLSQGAKP GKGGILPGAK VTSEIAKIRG IKPGQDCVSP NAHSEFKDVE GLINFIEKIA
     EQTGLPVGIK SAVGETKFWE ELAKRMKETG KGPDFITIDG GEGGTGAAPL TFTDHVSLPF
     KVGFARVYTI FQEEKLSDNI VWIGSGKLGF PDRTIIAFAM GCDLIHVARE AMMSIGCIQA
     QKCHTGHCPT GIATQSKWLQ AGLDVSIKAD RAANYIKGFR KELLSVAHAC GYEHPLQFTG
     HDIEIGAGQN RFRTLTEVLQ YEREPVRFTT MMDYTSFIPQ KT
//
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