ID J6J0Q8_9RHOB Unreviewed; 1573 AA.
AC J6J0Q8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:EJW10660.1};
GN ORFNames=A33M_4165 {ECO:0000313|EMBL:EJW10660.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW10660.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW10660.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW10660.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
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}.
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:EJW10660.1}.
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DR EMBL; AKZI01000089; EJW10660.1; -; Genomic_DNA.
DR RefSeq; WP_008388571.1; NZ_AKZI01000089.1.
DR STRING; 1187851.A33M_4165; -.
DR PATRIC; fig|1187851.3.peg.3096; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000002930; 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:UP000002930}.
FT DOMAIN 48..447
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1573 AA; 172463 MW; 87FEB539375C4EAE CRC64;
MSANGSGFSH DHLRAARPAT AEVATPVTTD AAARARGLYD PALEKDSCGV GFIADIKGRK
SHKIVEDALA ILCNLEHRGA VGADPRAGDG AGILVQMPHA FFAKKTEELG FRLPAPGRYA
VAQVFLPHDE ERRAEIMELF RANAARESMV VLGFRDVPTD DASLGESVKP TEPFHRQIFI
GQGERHYSED EFERRLYILR KTISRALYER RGRDTAMYYP VSFSCRTVIY KGMFLADQLG
KYYPDLSDPD FESALALVHQ RFSTNTFPTW SLAHPYRYVA HNGEINTLRG NVNWMAARQH
SARSPKYGDD IERLWPISYE GQSDTACFDN ALEFLVQGGY SLAHAVMMMI PEAWAGNPLM
DAHRRAFYEY HAALMEPWDG PAAIAFTDGR QIGATLDRNG LRPARYLVTR DDRILMASEM
GVLNIPEKDI VCKWRLQPGK MLLVDLAQGR LIPDDEIKAT LAQKHPYHEW LSRTQLVLED
LPPAKSCPVF PASGLLDRQQ AFGYSQEDLR ILMAPMGATG EEAIGSMGND TPISALSRRP
KLLFTYFKQN FAQVTNPPID PIREDIVMSL VSIIGPRPNL FDLEGLSKTM RLEARQPILS
NQDLEKIRSI ADMDGSQFRS ITLDVTWPAA DGADGLRPAI RELCAKAEQA VLDGFNIVIL
SDRAVSADRI PIPSLLACAA VHHHLIREGL RTSVGLVVES GEPREVHHFA CLAGYGAEAI
NPYLAFETLL SIRGELPSKP DEKEVVKRYV KSVGKGIKKV MSKMGISTYQ SYCGAQIFDA
VGLSSEFVHD YFTGTATRIE GAGLDEIAEE TVARHRDAFG DAPIYRNALD VGGEYAWRQR
GEEHVWTSAT VATLQHAVRG NSYDRYRAFA AMVNEQSEKL LTIRGLFRIK SAEQAGRTKV
PLDEVEPAAA IVRRFATGAM SYGSISREAH TTLAIAMNRI GGKSNTGEGG EEPDRFKPLP
NGDSMRSAIK QVASGRFGVT TEYLVNSDMM QIKMAQGAKP GEGGQLPGHK VDKVIARVRH
STPGVGLISP PPHHDIYSIE DLAQLIFDLK NVNPNGDVSV KLVSEVGVGT VAAGVSKARA
DHVTISGYEG GTGASPLTSI KHAGSPWEIG LAETHQTLVA NRLRGRIAVQ VDGGLRTGRD
VVIGALLGAD EFGFATAPLI AAGCIMMRKC HLNTCPVGVA TQDPVLRARF KGAPEHVINY
FFFVAEEVRE LMAEMGFRRF DEMIGQMQML DQRRMIEHWK AKGLDFSRLF MKPEAPAGVH
IFKSEVQDHK LDLVLDRKLI AEAQPALDRG APVRIVSEVH NTDRTVGAML SGEVARRYGH
AGLPDDTVHI RLSGTAGQSF GAWLAHGVTL ELEGDGNDYV GKGLSGGRIV VKPQSNSGIV
PEESIIVGNT VLYGAISGEC YFRGVAGERF AVRNSGATAV VEGAGDHCCE YMTGGVVVVL
GPTGRNFAAG MSGGIAYVLD EDGSFPSRCN MAMVELEPLP AEEAVNAAAY HHVRDLESAG
RVEVRQDMTR YDCERLHLLI SRHARFAGSR RAQQILDDWS SYLPKFRKVM PVEYKRALAE
LAKEKQAAMQ AAE
//
