ID A0A238WSK2_9RHOB Unreviewed; 1511 AA.
AC A0A238WSK2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:SNR49368.1};
GN ORFNames=SAMN06265370_10754 {ECO:0000313|EMBL:SNR49368.1};
OS Puniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR49368.1, ECO:0000313|Proteomes:UP000198417};
RN [1] {ECO:0000313|EMBL:SNR49368.1, ECO:0000313|Proteomes:UP000198417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR49368.1,
RC ECO:0000313|Proteomes:UP000198417};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNN01000007; SNR49368.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000198417; Unassembled WGS sequence.
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:UP000198417}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 164290 MW; 3914214F7A28578C CRC64;
MTKYDADWVR AEEAKRKWMT ENGLYAADEE HSSCGVGLVV SIDGKPSRRV VEAGISALKA
IWHRGAVDAD GKTGDGAGIH VQIPVSFFYD QIDRTGHTPR KNELMAVGQV FLPRTDFGAQ
ETCRTIVESE VLRMGHYIYG WRHVPVNVEC LGDKANATRP EIEQILISNA KGVDEETFER
ELYVIRRRIE KAAAAQGVGQ LYIASLSCRS IIYKGMMLAQ DVAEFYPDLM DERFESAFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT LKGNVNWMKS HEIRMASATF GEMADDIKPI
IANGASDSAA LDAVFEVLVR AGRNAPMAKT MLVPESWSKQ ALELPEAWRD MYSYCNSVME
PWDGPAALAM TDGRWVCGGL DRNGLRPMRY VVTGDGLLIA GSEAGMVPVD EGSVREKGAL
GPGQLIAVDM KEGKLFHDVD IKDKLAASQP FGEWVGKINE LDEELEKVSE KAMFSGAELR
RRQIAAGFTI EELEQILAPM AEDGKETIVS MGDDTPSAVL SKKYRPLSHY FRQNFSQVTN
PPIDSLREFR VMSLKTRFGN LKNVLDESSA QTEILVLDSP FVGNAQFDDL KRHFNADSVE
IDCTFPVGGS KEGLRRSLDR IRAEAEDAVR SGAGHLTLTD HLASEDKVAM PMILATSAVH
SHLTRKGLRT FCSINVRSAE CIDPHYFAVL IGAGATVVNP YLAADSLADR IERGLLDMTL
TQAVRKYREA IDQGLLKIMS KMGISVISSY RGGLNFEAVG LSRAMCAEFF PGMISRISGI
GVSGIQTKAE EIHRLGFLGG QDVLPIGGFY KSRKSGETHA WGAQNMHLLQ AACDKASYEL
WKTYSKAMQA NPPIHLRDLL AMKPIGPAIP LEQVESITSI RKRFVTPGMS LGALGPEAHK
TLNVAMNRIG AKSDSGEGGE DPAHFVPESN GDNPSAKIKQ VASGRFGVTA EYLNQCEELE
IKVAQGAKPG EGGQLPGMKV TKLIARLRHS TEGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRCKVTVK LVASSGVGTI AAGVAKAKAD VILISGHNGG TGASPATSIK YAGLPWEMGL
TEAHQVLSMN NLRERVTLRT DGGLRTGRDI VMAAMLGAEE YGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDEELRKKFT GTADKVVNLI TFYATEVREI LASIGARSLE DVIGRADLLR
QVSRGSDHLD DLDLNPLLIR VDGSDDIVYN RDRPRNAVPD TLDAEIVRDA ARFLEDGEKM
QLSYAVQNTH RTVGTRTSSH IVRKFGMRNS LQPDHLTVKL TGSAGQSLGA FAAPGLKLEV
SGDANDYVGK GLSGGIIVVR PPMHSPLVAS ENTIIGNTVL YGATEGYLFA AGRAGERFAV
RNSGASVVVE GCGSNGCEYM TGGIAVILGS VGANFGAGMT GGMAYLYDPE GIATVLMNME
SIVTCPVTVQ PWQDELRALI ERHAKETGSR KALDILQHWS EELPKFLQIC PKEMLNKIAH
PLTAGDSAVT A
//