ID K0UAF7_MYCVA Unreviewed; 1392 AA.
AC K0UAF7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:EJZ04342.1};
GN ORFNames=MVAC_29243 {ECO:0000313|EMBL:EJZ04342.1};
OS Mycolicibacterium vaccae ATCC 25954.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ04342.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ04342.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ04342.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL J. Bacteriol. 194:6339-6340(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}.
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:EJZ04342.1}.
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DR EMBL; ALQA01000125; EJZ04342.1; -; Genomic_DNA.
DR PATRIC; fig|1194972.3.peg.5791; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000006072; 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}.
FT DOMAIN 1..292
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1392 AA; 151482 MW; 555367B59E9A7F14 CRC64;
MLGWREMPVD PDGAELGATA RNCMPHMAQL FVAAPEDHGV RPAGIDLDRR VYPVRKRAER
AGVYFPSLSS RTMVYKGMLT TMQLPQFFSD LRDERCVSAI AIVHSRFSTN TFPSWPLAHP
FRFVAHNGEI NTVRGNRNRM HAREAKLASA GIPGDLSRLS PICTPDASDS ASFDEVLELL
HLGGRSLPHA VLMMIPEAWE NSATMDPAER AFWQFHASLM EPWDGPACVT FTDGTLVGAV
LDRNGLRPGR WWRTINDRII LASEAGVLDV PSAEIVAKGR LQPGKMFLID TAAGRIVSDD
EIKEKLAHAE PYGEWLHAGL LELKTLPHRT RVQPNHESVV RRQVSFGYTE EDLRILLTPM
AASGAEPLGS MGTDTPTAVL SQRSKLLYDY FVELFAQVTN PPLDAIREEI VTSMSRIMGP
EQNLLEPSAA SCRQIKLTWP VLDNDDLNKI VHINADGEHP GLRTAVLRAL YDVERGGEAL
AEALEELRLR ASDAIAKGAR TLVISDRDSD HTKAPIPSLL AVSAVHHHLV RTKERTTVAL
VVESGDAREV HHIAMLIGFG AAAVNPYLAF ESIEDLIREG ELTGIEPATA VRNYTKALGK
GVMKVMSKMG ISTVASYTAA QAFEAIGIDK GVIDEYFTGT PTQLGGVGLD VIAEEVKLRH
RRAYPENPTE RVHRRLEVGG EYAFRREGEL HLFTPEVVFL LQHSTRTGRH EVFEKYSAEV
DRLAREGGAL RGLFEFKKGV RPPVPLDEVE SVESIVTRFN TGAMSYGSIS AEAHETMAVA
MNKLGGRSNS GEGGEDVDRL YDPQRRSAVK QVASGRFGVT SDYLVNATDI QIKMAQGAKP
GEGGQLPGYK VYPNIAKTRH ATPGVSLISP PPHHDIYSIE DLAQLIHDLK NANSEARIHV
KLVSSVGVGT VAAGVSKAHA DVVLISGYDG GTGAAPLTSL KHAGAPWEIG LADTQQTLML
NGLRDRITVQ CDGGMRTARD VMVAMLLGAE EYGFATAPLV VSGCIMMRVC HLDTCPVGVA
TQNPELRARY TGKPEFVENF FRFIAEDIRR YLAELGFRSV DEAVGRAEML DTAAGVAHWK
SQGLDLTPIF AVPADAHTGQ PAARRRVHEQ YHALDQALDQ TLIQLAEGAL EDAHPVRLEL
PIRNVNRTVG TLLGSEITRR YGAQGLPEDT VHITLTGSAG QSLGAFLPPG VTLELVGDAN
DYVGKGLSGG KIVVKPQDDV LFLPEDNVIA GNTLLFGATA GELYLRGRVG ERFAARNSGA
LTVVEGVGDH ACEYMTGGRV VVLGKVGRNM AAGMSGGIAY VLGLDPSRVN TEMVELQRLE
PEDLSWLHDV VARHARYTGS TVATSVLSDW PRRSAQFTKI MPRDYQRVLQ ATRMAQAEGR
DVDSAIMEAS RG
//
