ID A0A1E5PCT4_9ACTN Unreviewed; 1519 AA.
AC A0A1E5PCT4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OEJ27340.1};
GN ORFNames=AS594_25540 {ECO:0000313|EMBL:OEJ27340.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ27340.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ27340.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ27340.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-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}.
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:OEJ27340.1}.
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DR EMBL; MEHJ01000001; OEJ27340.1; -; Genomic_DNA.
DR RefSeq; WP_069935395.1; NZ_MEHJ01000001.1.
DR STRING; 285458.BGM19_11385; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000095759; 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:UP000095759}.
FT DOMAIN 28..412
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"
SQ SEQUENCE 1519 AA; 163389 MW; AD19B7279AC0A003 CRC64;
MRSDAWSPMD GRPAQQGMYD PRNEHDACGV GFVATLTGVA SHELVEQALT VLRNLEHRGA
TGSEPDSGDG AGILLQVPDA FLREVTAFDL PEAGAYAVGI GFLPADGSAQ AVSRIEAIAA
EEGLDVLGWR EVPVTPQLLG NGARATMPAF GQLFVADGTS TGLELDRKAF VLRKRAERET
GVYFPSLSAR TIVYKGMLTT GQLEPFFPDL SDRRFATTVA LVHSRFSTNT FPSWPLAHPY
RFVAHNGEIN TVKGNRNWMK ARESQLASDL FGADKLERIF PVCTPDASDS ASFDEVLELL
HLGGRSLPHA VLMMVPEAWE NHDSMDPARR AFYQYHATMM EPWDGPACVT FTDGTQVGAV
LDRNGLRPGR YWVTDDGLVV LSSEVGVLDI DPAKVVRKGR LQPGKMFLVD TAEHRIIEDD
EIKAGLAAEA PYQEWLEAGE IELEDLPERE HIVHTHASVT RRQQTFGYTE EELRVILAPM
ARTGGEPLGS MGTDSPIAAL SERPRLLFDY FTQLFAQVTN PPLDAIREEL VTSLRSSLGP
QGNILEPTAA TCRNVTLPFP VIDNDELAKL IHINADGDMP GMTAATLSGL YRVSGGGDAL
AARIEEICAE ADAAIEAGAR LIVLSDRHSD AEHAPIPSLL LTSAVHHHLI RTKQRTQVGL
LVEAGDVREV HHVALLIGFG AAAVNPYLAM ESVEDLVRAG TFIEGAEPEQ AIRNLIYALG
KGVLKVMSKM GISTVASYRG AQVFEAVGLD EAFVEKYFNG TATKIGGAGL DVVAKEVAAR
HAKAYPASGI AASHRALEIG GEYQWRREGE PHLFDPETVF RLQHATRGRR YDIFKQYTDR
VNEQSERLMT LRGLFGFKSG RTPISIDEVE PVSEIVKRFS TGAMSYGSIS QEAHETLAIA
MNQLGGKSNT GEGGEDAERL YDPARRSSIK QVASGRFGVT SEYLVNADDI QIKMAQGAKP
GEGGQLPGHK VYPWVAKTRH STPGVGLISP PPHHDIYSIE DLAQLIHDLK NANPAARIHV
KLVSEVGVGT VAAGVSKAHA DVVLISGHDG GTGASPLTSL KHAGGPWELG LAETQQTLLL
NGLRDRIVVQ TDGQLKTGRD VIIAALLGAE EFGFATAPLV VSGCVMMRVC HLDTCPVGIA
TQNPVLRDRF SGKAEYVVNF FQFIAEEVRE LLAELGFRTL EEAVGHAELL DTDAAVDHWK
AQGLDLEPLF YVPELPEGAV RHQVTTQDHA LEKALDNELI KLAADALAVD SAEAAGPVRA
QVAIRNINRT VGTMLGHEVT KKFGGAGLPD DTIDITFTGS AGQSFGAFVP RGVTLRLEGD
ANDYVGKGLS GGRIIVRPDR GADHLAEYST IAGNTIAYGA TSGELFLRGR TGERFCVRNS
GATVVSEGVG DHGCEYMTGG RAVVLGETGR NFAAGMSGGV AYVIDLDPDN VNSGNAGAVE
ALDDTDKLWL HDVVRRHEEE TGSTVASKLL AEWDTAVARF SKIIPSTYKA VLAAKDAAEL
AGLSEQETTE KMMEAATNG
//
