ID L7LQU8_9ACTN Unreviewed; 1544 AA.
AC L7LQU8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:GAC62552.1};
GN Name=gltB {ECO:0000313|EMBL:GAC62552.1};
GN ORFNames=GSI01S_37_00350 {ECO:0000313|EMBL:GAC62552.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC62552.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC62552.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC62552.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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:GAC62552.1}.
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DR EMBL; BANU01000037; GAC62552.1; -; Genomic_DNA.
DR RefSeq; WP_006897965.1; NZ_BANU01000037.1.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR Proteomes; UP000035083; 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:UP000035083}.
FT DOMAIN 20..428
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1544 AA; 166913 MW; AE85ECAE1850B77F CRC64;
MKHLPGPVGL YDPINEHDAC GVAFVVDMHG RRSRDIVEKA ITALVNLEHR GAAGAEPNTG
DGAGIMIQVP DRFLREVVDF DLPAEGSYAT GIAFLPQSAG DAAEAVEGVE EIIAAEGLTL
LGWRDVPVDE SSLGALARDA MPTFRQVFLA LAGSEASGRT PSSAEIMELE RKAYVVRKRV
QYELGEKGAG QDGPGRDTVY FPSLSGQTFV YKGMLTTPQL RDFYLDLQDE RVESALGMVH
SRFSTNTFPS WPLAHPFRRV AHNGEINTVS GNENWMRARE SLIKTDVFGD SLDKVFPVCT
PGASDTARFD EVLELLHLGG RTLPHAVLMM VPEAWERSED MKPEHRAFYE YHSALMEAWD
GPASVCFTDG TVIGAVLDRN GLRPSRIWVT KDGLVVLGSE VGVLDIDPAD VVAKQRLQPG
KMFLVDTAQG RIVADEEIKD SLAGEQPYQE WLDANQVALS DLPAPPHKHM AHDRVTLRQQ
MFGYTTEDLK LLISPMAATG GEALGSMGTD TPVAVLSNRP RMLFDYFQQL FAQVTNPPLD
AIREEVVTSL GGRIGGERDL LNPAAGSAKQ IVLSQPILDN DDLARLVEID PATGFPSVHI
HGLYPVAEGG EGLRRALDGV RSKVSAAIAD GARIIVLSDR ESDETLAPIP SLLLTAAVHH
HMVRERTRTR ASLIIESGDA REVHHMALLV GFGASGINPY MAFETIEDML ESGSLDVPGT
EDMSHEATFA VARANYIKAA GKGVLKVMSK MGISTVPSYT GAQLFQVIGL GQEVVDEFFT
GLNSQLDGIG LDEIADEVAQ RHALAFTKRP AERAHRELEV GGEYQWRREG EYHLFNPDTV
FKLQHSTRTG QYSVFKEYTK LVDDQAAKLG TLRGLFDFNF GDRDPIPIDK VEPASEIVKR
FSTGAMSYGS ISAEAHETLA IAMNRLGGRS NSGEGGEDPR RFVHDENGDW RRSAIKQVAS
GRFGVTSHYL SNCTDIQIKM AQGAKPGEGG QLPPHKVYPW VAEVRGSTPG VGLISPPPHH
DIYSIEDLAQ LIHDLKNANP QARIHVKLVS ELGVGTVAAG VSKAHADVVL ISGHDGGTGA
SPLTSLKHAG APWEIGLAET QQTLLLNGLR DRIVVQVDGQ LKTGRDVMIA ALLGGEEFGF
ATAPLVVSGC IMMRVCHLDT CPVGVATQNP LLRERFSGKP EFVENFMLYV AEEVRELLAR
LGFRTLQEAV GRFEALDTRK ALEHWKNHKA GKLDLTPILT MPESPFMNQD LYCSGTQDHG
LDKALDNELI EKARAAIESG TRVTLASPIS NVNRTVGTML GHEVTKAYGA QGLPEGTISI
DFTGSAGNSF GAFVPRGITM RIEGDANDFV GKGLSGGKIV VRPPRNAPAE FVAEDNIIGG
NVIAFGGTAG KIFLRGVVGE RFCVRNSGVQ AVVEGVGDHG CEYMTGGTAV ILGRTGRNFA
AGMSGGVAYV YNPHGEFEAD LNTELVELEE LDADDLTVLS GLLTEHRDET GSPVAAAILD
DWDVARGHFV KVMPRDYKKV LVAIDAAERS GRDVNEAIME AARG
//
