ID A0A1T0CNQ2_9GAMM Unreviewed; 558 AA.
AC A0A1T0CNQ2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:OOS23889.1};
GN ORFNames=B0681_07940 {ECO:0000313|EMBL:OOS23889.1};
OS Moraxella porci DSM 25326.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=573983 {ECO:0000313|EMBL:OOS23889.1, ECO:0000313|Proteomes:UP000190683};
RN [1] {ECO:0000313|EMBL:OOS23889.1, ECO:0000313|Proteomes:UP000190683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 54912 {ECO:0000313|EMBL:OOS23889.1,
RC ECO:0000313|Proteomes:UP000190683};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella porci CCUG 54912T type strain.";
RL Submitted (FEB-2017) 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:OOS23889.1}.
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DR EMBL; MUYV01000011; OOS23889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CNQ2; -.
DR STRING; 573983.B0681_07940; -.
DR Proteomes; UP000190683; 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 InterPro; IPR027283; YerD.
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 PIRSF; PIRSF500060; UCP500060; 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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 165..480
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
SQ SEQUENCE 558 AA; 62381 MW; C53046095B646615 CRC64;
MPNLKPDNHS ANFFFLVLPR FALFWVCVAL IPISILFKIW WLLFIATCLT CLGVYNIHQK
RHAILRNYPI SGHIRFLFEN FRPEVRQYFI EGDREEVPFS RLQRSIVYQR AKDLDSTTAF
GSLNDLSKPG TDWFLHSGRS HKIDNHDFRV RVGNERCLQP YDLSVFNISA MSFGALSANA
IEALNKGAKE GGFAHDTGEG SISPYHQKHG GDLIWQLGTA YFGCRDEHGR FNPETFAERA
KSPQVKMIEI KLSQGAKPGK GGVLPATKIT HEIAATRDIP MDIDCISPPT HPEFSTPKQL
VEFWQRLRDL SGGKPVGIKL CIGMPWEFMA IVKAMKEENN YPDFIVIDGA EGGTGAAPVE
FMDSVGMPLV DALIFVQNTL VGAGIRDKIK VGVSGKVITA FDIAKMMALG ADWCNSARGF
MFAVGCIQSR SCHTNKCPTG VATQDPARQK ALDVPDKSRR VKNYHHNTLK ALAEIVGCSG
LDHPSQLMPH HIVRRQPDGW IKLLSEHYQF IEHGSLLTGD SGRRVLDDMW KLADSNSFQA
MTIADEIVDA ENERNRML
//