ID A0A1B1PMM8_9RHOB Unreviewed; 1513 AA.
AC A0A1B1PMM8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:ANT59857.1};
GN ORFNames=AYJ57_05410 {ECO:0000313|EMBL:ANT59857.1};
OS Salipiger sp. CCB-MM3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT59857.1, ECO:0000313|Proteomes:UP000092483};
RN [1] {ECO:0000313|EMBL:ANT59857.1, ECO:0000313|Proteomes:UP000092483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT59857.1,
RC ECO:0000313|Proteomes:UP000092483};
RA Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT Yangia sp. CCB-MM3.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CP014595; ANT59857.1; -; Genomic_DNA.
DR RefSeq; WP_066102283.1; NZ_CP014595.1.
DR STRING; 1792508.AYJ57_05410; -.
DR KEGG; yan:AYJ57_05410; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000092483; Chromosome 1.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092483}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 163961 MW; 7CD97F56B9E0D09F CRC64;
MTTFDANWVA AEEAKRKWME ENGLFREEHE HSSCGVGLVV SIDGKPSRKV VEAGITALKA
IWHRGAVDAD GKTGDGAGIH VQIPVSFFYD QIERTGHAPR KGELMAVGQV FLPRTDFGAQ
ETCRTIVETE VLRMGHYIYG WRHVPVSVEC LGEKANATRP EIEQILISNA KGVDEETFER
ELYVIRRRIE KAAAAAGING LYIASLSCRS IIYKGMMLAE QVAVFYPDLQ DERFESAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT IKGNTNWMKS HEIRMASATF GEMAEDIKPI
IAHGASDSAA LDAVFEVLVR AGRNAPMAKT MLIPEAWSKQ AVELPQAWLD MYSYVNSVME
PWDGPAALAM TDGRWVCGGL DRNGLRPMRY VVTGDGLLIA GSEAGMVPVD ESTVREKGAL
GPGQLIAVDM EEGKLYHDTE IKDRLAASQP FGEWVGKITE LDESLGKVAE KPLFTGGELR
KRQIAAGYSI EELEQSLSAM AEDGKEMLAS MGDDTPSAVL SKKYRPLSHF FRQNFSQVTN
PPIDSLREFR VMSLKTRFGN LKNVLDESSA QTEILVLDTP FVANAQFDEL TQHFNAGLVE
IDCTFPAGAG EGALRDGLAR IRAEAEDAVR SGGGHIVLTD HHQGEGKVAM PMILATSAVH
SWLTKKGLRT FCSLGVRSAE CIDPHYFAVL VGCGATIVNP YLAEDSIADR IERGLLDGSL
TENVARYREA IDQGLLKIMS KMGISVISSY RGGLNFEAVG LSRAMCAEYF PGMLSRISGI
GVHGIQQKAE EVHALGFKGG RDVLPIGGFY KARKSGETHA WGAQSMHLMQ AACNKSSYEL
WKTYSKAMRA NPPIHLRDLL DFKPMGNAIP LEEVESITSI RKRFVTPGMS LGALSPEAHK
TLNVAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKIKQ VASGRFGVTA EYLNHCEELE
IKVAQGAKPG EGGQLPGMKV TELIAKLRHS TKGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRCKVTVK LVASSGVGTI AAGVAKAKAD VILISGHNGG TGASPATSIK YAGLPWEMGL
TEAHQVLAMN KLRDRVTLRT DGGLRTGRDI VMAAMLGAEE FGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDPELRDKFT GNAEKVVNLI TFYATEVREI LASIGARSLN DVIGRADLLS
QVSRGAEHLD DLDLNPLLIR VDGADDIVYD RSKGRNVVPD TLDAEIVRDG SRFLEDGEKM
QLSYAVQNTH RTVGTRTSSH IVSKFGMRNA LQPDHLHVKL TGSAGQSLGA FAAPGLKLEV
SGDANDYVGK GLSGGTIVVR PPMMSPLTAS ENTIIGNTVL YGATDGYLFA AGKAGERFAV
RNSGATVVVE GCGTNGCEYM TGGLAVILGP IGANFGAGMT GGMAYLYDPE GLAPDLMNME
SLVTCPVAEE HWEAELKGMV ERHAQETGSR KALDILQNWV TEKDKFLQVC PREMLDKIAH
PLGIEQDMAV PAE
//
