ID M2XAP9_9MICC Unreviewed; 637 AA.
AC M2XAP9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ferredoxin-dependent glutamate synthase {ECO:0000313|EMBL:EME36166.1};
GN ORFNames=C884_00645 {ECO:0000313|EMBL:EME36166.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME36166.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME36166.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME36166.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME36166.1}.
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DR EMBL; ANHZ02000017; EME36166.1; -; Genomic_DNA.
DR RefSeq; WP_006215068.1; NZ_ANHZ02000017.1.
DR AlphaFoldDB; M2XAP9; -.
DR STRING; 71999.KPaMU14_04560; -.
DR Proteomes; UP000009877; 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 Reference proteome {ECO:0000313|Proteomes:UP000009877};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..471
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT REGION 557..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 68652 MW; EB519F6BC974599A CRC64;
MNNRFLMAGA VVTLALVLLV AYLVGMWAWI FLGVVALLLL GLGIWDLVQP RHAILRNFPV
LGHARYLLES IRPEIQQYFI EKNTEGKPFS RDQRSIVYAR AKGQDDHKAF GTEKATDEIG
YEFLLHTTAP VAPAAEPPTV RVGGPDCAQP YEMPLMSISS MSFGSLSKNA VLAMNKGAAM
GGFVHETGEG GLTEYHLGNG ADLFWEIGSG YFGCRYDDGR FNPERFAEKA RYDEVKGITI
KLSQGAKPGL GGVLPGSKVT AEIAEAREVP EGVDCISPAS HSAFTTPREM VRFIGQLREL
SGGKPIGIKF CVGSRTDVLA MCKAMWEERI APDYIIVDGS EGGTGAAPLE YSDHVGTPLT
EGLMLVHNAL VGTGLRHMIR IGAAGKVVSG SDIVKRMIQG ADFTMSARGM MMATGCIQAQ
KCHTNHCPVG VATQDARLMR ALDVEDKAKR VHNYQKLTVR EAVQIMASMG VEAPSQLNAR
MLRRRVDHLN TRSYASIYNW LREGELLEQP PRGWAADWAE ADADHFGEHA PLGFLDDDGP
HWNDEMATQT GMMATVGAGS SLASSGGSHA PGGPSGERHS EAHTASGTRS GEQEQGQQPV
RSDGDEPIGR PEASRTPTTG STPVVGDSTR PEGRPAE
//
