ID M1NUS3_9CORY Unreviewed; 1528 AA.
AC M1NUS3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN ORFNames=A605_01255 {ECO:0000313|EMBL:AGF71265.1};
OS Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF71265.1, ECO:0000313|Proteomes:UP000011723};
RN [1] {ECO:0000313|EMBL:AGF71265.1, ECO:0000313|Proteomes:UP000011723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF71265.1};
RX PubMed=23408721;
RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA Kalinowski J.;
RT "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT type strain YIM 70093(T) (= DSM 44683(T)).";
RL Stand. Genomic Sci. 7:284-293(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}.
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DR EMBL; CP003697; AGF71265.1; -; Genomic_DNA.
DR RefSeq; WP_015399689.1; NZ_JIAJ01000002.1.
DR STRING; 1121362.A605_01255; -.
DR KEGG; chn:A605_01255; -.
DR PATRIC; fig|1121362.3.peg.242; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000011723; Chromosome.
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:UP000011723}.
FT DOMAIN 16..410
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1528 AA; 165473 MW; F95C19BD2A20ED33 CRC64;
MNREGLYNPA HEHDACGVGF VADLHGRPSR AIVDKGLQVL INIDHRGAAG AERNTGDGTG
ILLQIPDRFY RDDMARQGVT LPAAGAYATG IAFLPRARMA MLDAKREIEA IAVEEGATVL
GWREVPVDPG ELGTMAHDAM PSFAQLFLSA GDRRGIDLDR VMFRIRKRCT RELGTKNGEE
TVYFPSLSAR TIVYKGMLTT PQLAQFYADL RDPRLESAIA LVHSRFSTNT FPSWPLAHPY
RFVAHNGEIN TVKGNENWMR ARESLIDSPL LGDLDRVLPV CTPGASDTAR FDEALELLHL
GGYSLPHAMA MMIPQAWEHN PTIDPALRDF HEYHSCLMEP WDGPAAVAFT DGTLVGAVLD
RNGLRPGRIW ITDDGLVVMA SEAGVLDIDP ARVVKRTRLQ PGKMFLLDTE AGRIVPDGEI
KRQLADARPY REWIRHNFVP LAGLPQTRYE YMPHDRAVLR QRVFGVTEED VDLIIRPMAL
DAAEAIGSMG SDTPIAALSQ RPRMLYDFFA QRFAQVTNPP LDSIREKPVT SMHTLLGAQS
DVLNPGPEAA RRIRLDSPVI DNHQLATLAH ADDHGEWPAF HTAVISGLYP VAHHGAGLRE
AIERVRREVS EAIAAGASII VLSDRESDER HAPIPSLLLT SAVHQHLVAG RTRTRCSLVI
ESGDAREVHH LAMLIGFGAD AINPYMAFET IDELRMAGQL GELTLDEACT NYVTAATSGV
LKVMSKMGIA TVASYRGAQL ADVTGLHSDL LDEYFGAVPS PVGGIGLEEL AADVEARHRG
AFLPRPEELA HRELELGGEY KWRREGEYHL FNPETIFKLQ HATKTGRYAI FKDYTAAVDR
QSQRLATLRG MMEFAPDRPP VPVEEVEPVA DIVQRFSTGA MSYGSISAEA HETLAIAMNR
LHAMSNSGEG GEDPARFEPE PDGDWKRSAI KQVASGRFGV TSHYLTNCTD IQIKMAQGAK
PGEGGQLPPN KVYPWIAEVR VTTPGVGLIS PPPHHDIYSI EDLAQLIFDL KNANPDARIH
VKLVSEQGVG TVAAGVSKAH ADVVLISGHD GGTGASPLTS LKHAGGPWEL GLAETQQTLL
LNGLRDRIRV QCDGQLKTGR DVVVATLLGA EEFGFATAPL VVEGCVMMRV CHLDTCPVGV
ATQNPDLRAK FTGRAEHVVN FFRFLAQEVR EYLAQLGFRS IDEAVGQAQV LRQSRDAEFT
AANPRAAALD LAPVFHVPRS RFRNQNPRRT RAQEHGLAGV LDERIIRDTQ LTIDAAAAAV
SENAPAWMSS GPAPTIAMSY PIRNVDRSVG TMAGSRVTRA AGRDGLPDGT VTLTFTGSAG
NSFGAFVPRG MTLDLVGDAN DFIGKGLSGG RLIVRPHAAA PGQIDAGEPD IIAGNVIGFG
ATAGEIFIAG SVGERFCVRN SGATAVVEGI GNHGCEYMTG GRVVVLGEVG DNFGAGMSGG
IAYLAPQPGL ERKINPELVD VETPTAADVE FLEGVIDEHI RVTGSTTPWQ ARDLVKVMPR
DYRKVLTIIS TAGAEGRDVD TAIMEAVN
//
