ID A0A143QF30_9NOCA Unreviewed; 1533 AA.
AC A0A143QF30;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:AMY21082.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AMY21082.1};
GN Name=gltB {ECO:0000313|EMBL:AMY21082.1};
GN ORFNames=A3Q40_03731 {ECO:0000313|EMBL:AMY21082.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY21082.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY21082.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY21082.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-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; CP015219; AMY21082.1; -; Genomic_DNA.
DR RefSeq; WP_068104373.1; NZ_CP015219.1.
DR STRING; 1653478.A3Q40_03731; -.
DR KEGG; rhu:A3Q40_03731; -.
DR PATRIC; fig|1653478.3.peg.3788; -.
DR Proteomes; UP000076180; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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 InterPro; IPR001202; WW_dom.
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.
DR PROSITE; PS50020; WW_DOMAIN_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 ECO:0000313|EMBL:AMY21082.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180}.
FT DOMAIN 24..426
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 327..362
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 922..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 166993 MW; 564172CA37B90379 CRC64;
MQIPGHRYPA AQGLYDPAHE HDSCGVAFVV DMYGRRSRDI VDKAITALVN LEHRGAAGAE
PNTGDGAGIL IQVPDAFYRA VVDFELPAEG AYATGIAFLP QARAAVQEAV EGVERIVVEE
GLEVLGWRTL ETDDTSLGAL ARDAMPTFRQ IFVAAPDRSL TGLDLERRAF VARKRVEHEL
GTEGPGKDGP GRESVYFPSL SPSTIVYKGM LTTPQLKGFY LDLQDERVES ALGLVHSRFS
TNTFPSWPLA HPFRRVAHNG EINTVTGNEN WMRAREALID SDAFGGREKL DAIFPVCTRG
ASDTARFDEV LEFLHLGGRS LPHAVLMMIP EAWEHHETMD PARRAFYQFH STLMEPWDGP
ASVCFTDGTV IGAVLDRNGL RPSRLWVTDD GLVVMASEVG VLDIEPSRIV KKVRLQPGRM
FLVDTAQGRI VSDDEIKDEL AAEHPYQEWL DQGLLTVDEL PERPHVHMSH DRVLIRQQIF
GYTTEELNVL LAPMAKTGAE AVGSMGTDTP VAVLSARPRM LFDYFSQLFA QVTNPPLDAI
REEVVTSLGG TIGPERDLLQ PTAEACRQIV LNSPILHNDE LAKLVHINDD GNLDELRSVV
VRGLYPVAEG GEGLRRSLEI IRAQVSAAIA GGARIVILSD RESNEKLAPI PSLLLTSAVH
HHLVREKTRT KVGLIVEAGD AREVHHMATL VGFGAAAVNP YMAFESIEDM IERGNLQGVE
YDAAVRNYIK AAGKGVLKVM SKMGISTLAS YTGAQLFQVI GLSQDLVDEY FHGVTSPLGG
IDLDQIAADV AARHGIAYLD NKFERAHREL ETGGEYQWRR EGEYHLFNPD TVFKLQHATR
TGQYRVFKEY TQMVDDQSER LASLRGLFRF RTEGRNPIPL EEVESAREIV KRFSTGAMSY
GSISAEAHET LAIAMNRLGG RSNSGEGGED VARFTPDENG DSRRSAIKQV ASGRFGVTSN
YLTNCTDIQI KMAQGAKPGE GGQLPAHKVY PWVAEVRHST PGVGLISPPP HHDIYSIEDL
AQLIHDLKNA NPSARIHVKL VSEIGVGTVA AGVSKAHADV VLISGHDGGT GATPLTSVKH
AGAPWELGLA ETQQTLLLNG LRDRIVVQVD GQLKTGRDVM VAALLGGEEF GFATAPLVVS
GCIMMRVCHL DTCPVGVATQ NPVLRKRFAG QPEFVENFFL YIAEEVREYL AEFGFRTLDE
AVGQVGLLDT TAAKEHWKAS KLDLSPILDQ PESAFMNQDL YCTGTQDHSL DKALDQQLIT
QSREALDSGE KVQFTTRITN VNRTVGTMLG HELTKKYGAD GLPDDTIDIT FTGSAGNSFG
AFVPKGMTLR LEGDANDFVG KGLSGGRIVV RPSRDANPDF VAENNIIAGN VILFGATEGE
ALIRGVVGER FAVRNSGATA VVEGVGDHGC EYMTGGKVVI LGETGRNFGA GMSGGVAFVF
DPNSTFEANL NTELVDIEAL EGDEFAWLKD AVTRHRDQTG SEVAERILAD WSQQVNHFVK
VMPRDYKKVL LAISEAEKNG ADVDEAIMEA ARG
//
