ID I4BJ61_MYCCN Unreviewed; 1513 AA.
AC I4BJ61;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Glutamate synthase family protein {ECO:0000313|EMBL:AFM17318.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:AFM17318.1};
GN OrderedLocusNames=Mycch_2545 {ECO:0000313|EMBL:AFM17318.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM17318.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM17318.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM17318.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-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}.
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DR EMBL; CP003053; AFM17318.1; -; Genomic_DNA.
DR RefSeq; WP_014815798.1; NC_018027.1.
DR STRING; 710421.Mycch_2545; -.
DR KEGG; mcb:Mycch_2545; -.
DR PATRIC; fig|710421.3.peg.2542; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000006057; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016040; F:glutamate synthase (NADH) 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 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 ECO:0000313|EMBL:AFM17318.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 22..418
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1513 AA; 164049 MW; 4630DC1010DD9A20 CRC64;
MLFSALPEPQ GLYDPGNESD SCGVAMVTDI QGRRSHSIVT DGLIALEHLE HRGAAGAEPN
SGDGAGILIQ VPVEFLRDVV DFDLPAPGVD GSNTFAAGIC FLPQDQTART HALGTVESIA
TEEGLEILGW REVPVDPDGA DVGVTALGCM PYMAQVFVAA SAHDGTRLGG IDLDRRVYPM
RKRSERTGVY FPSLSSRTIV YKGMLTTMQL PQYFPDLRDE RCVSAIAIVH SRFSTNTFPS
WPLAHPFRFV AHNGEINTVR GNRNRMHARE AMLASTKIPG DLNRLSPICT PDASDSASFD
EVLELLHLGG RSLPHAVLMM IPEAWENSDT MDPAERAFWQ FHASLMEPWD GPACVTFTDG
TLVGAVLDRN GLRPGRWWRT IDDRIILASE SGVLDVPSAE VVAKGRLQPG KMFLIDTAAG
RIISDDEVKE SLAKAEPYGE WLHAGLLDLT ALPDRVRVQP NHESVVRRQI SFGYTEEDLR
ILLTPMAASG AEPLGSMGTD TPAAVLSQRS KLLYDYFIEL FAQVTNPPLD AIREEVVTSM
ARIMGPEQNL LEPSAASCRQ IRLNWPVLDN DELNKIVHIN DDGEQPGLRT AVLKALYEVE
RGGEGLAEAL DDLRLRACDA IARGARTLVI SDRDSDHTKA PIPSLLAVSA VHHHLVRTKQ
RTTVALVVET GDAREVHHIA MLIGFGAAAV NPYLAFESIE DLIREGELTG IEPAAAVRNY
LKALGKGVMK VMSKMGISTV ASYTAAQAFE AVGIDRDVID EYFTGTPTQL GGIGLDVIAE
EVKLRHRRAY PENPTERVHR RLEVGGEYAF RREGELHLFT PEVVFLLQHS TRTGRYDVFE
KYSDEVNRLA REGGALRGLF DFRKGLRPPV PLDEVESVES IVKRFNTGAM SYGSISAEAH
ETMAIAMNKI GGRSNSGEGG EDADRLYDPT RRSAVKQVAS GRFGVTSDYL VNASDIQIKM
AQGAKPGEGG QLPAYKVYPN IAKTRHSTPG VGLISPPPHH DIYSIEDLAQ LIHDLKNANA
DARVHVKLVS SVGVGTVAAG VSKAHADVVL ISGYDGGTGA APLTSLKHAG APWEIGLADA
QQTLMLNGLR DRITVQCDGG MRTARDVMVA MLLGAEEYGF ATAPLVVAGC IMMRVCHLDT
CPVGVATQNP ELRARFNGKP EFVENFFQFI AEDIRRYLAE LGFRSIDEAV GHAEVLDTDM
GVAHWKSRGL DLTPIFAVPA GDGPRRKVRE QDHGLGQALD RTLIQLAEGA LEDAHPVRLE
LPVRNVNRTV GTLLGSEVTR RYGAQGLPDD TIHVTLTGSA GQSIGAFLPP GITLELIGDA
NDYVGKGLSG GRVIVKPQDD VLFLPEDNVI AGNTLLYGAT SGEVYLRGRV GERFAARNSG
ALAVVEGVGD HACEYMTGGR VVVLGKVGRN MAAGMSGGIA FVLGLDPRRV NTDMVELQDL
EPEDLAWLRE VIAQHAHVTD STVATSVLSD WPRRSAQFTK IMPRDYQRVL QATRMAKAEG
RDVDTAIMEA SRG
//
