ID D7UU74_LISGR Unreviewed; 1540 AA.
AC D7UU74;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Class II glutamine amidotransferase {ECO:0000313|EMBL:EFI85322.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:EFI85322.1};
GN Name=gltB {ECO:0000313|EMBL:EFI85322.1};
GN ORFNames=HMPREF0556_10049 {ECO:0000313|EMBL:EFI85322.1};
OS Listeria grayi DSM 20601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI85322.1, ECO:0000313|Proteomes:UP000010119};
RN [1] {ECO:0000313|EMBL:EFI85322.1, ECO:0000313|Proteomes:UP000010119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI85322.1,
RC ECO:0000313|Proteomes:UP000010119};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) 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:EFI85322.1}.
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DR EMBL; ACCR02000001; EFI85322.1; -; Genomic_DNA.
DR STRING; 525367.HMPREF0556_10049; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_9; -.
DR Proteomes; UP000010119; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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 Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
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 ECO:0000313|EMBL:EFI85322.1}; 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:EFI85322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW Transferase {ECO:0000313|EMBL:EFI85322.1}.
FT DOMAIN 31..427
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT COILED 603..630
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1540 AA; 171557 MW; 44E4CB89CD792A7E CRC64;
MALKEEEPLM KVTNLPEKHG LYDPSREHDA CGIGFVANIK HRDSHKIVEQ GIHMLCQLKH
RGGELGGDTG DGAGILLEIS DSFFRHVCLE MGIELPAKYT YAVGMFNFPQ DSAQRELLMA
EAEKLIQQER QHFLGWRKVP TDASKVGAGA RETEPAIYQL FVEQERGLTE REFEKQLYLI
RRQIENFAAN SKAVTEVFYI PSLSTRTVIF KGMLTPEQID RYYLDLADPA YTSSFAFVHS
RFSTNTFPSW ERAHPYRYLV HNGEINTQRG NVNWMKAREK RAASSLFGDD LAKVIPVIDE
NGSDSAALDN ALEFLVQTGR SLPHAAMMLI PEPWDKNPNM LDPKRAFYEY HSMLMEPWDG
PTSISFTDGR VIGTILDRNG LRPARYYETK DHTIIYSSET GVVPVEAEEV IRKETVGAGE
MLFIDLEQGK LITDKEVKMH LTAAKPYREW LKAELTELAD LAKAEPSEQA ELSKSERFKE
QRAFGYTQDE LNKILIPMVT EKKDPMGAMG YDAPLAVLSQ RPQLLFNYFK QLFAQVTNPP
IDGIREEVVT SSMTLLGDEG NILEPSAKNA HRIRLATPVL KRAEFQALME QNVFTKKTRK
IAIHFSEKER DQLEARLQEV FEEAAEAIRD GAELLVLSDR GVNDDRIGIP SLLVTSGLHH
YLVQQGLRTK ASLVLETAEA RDVHHLSLLV GYGADAVYPY LAIDTIAGLI DEQRIKGFTL
QEAEQRYAEA LTDGMLKVMS KMGISTVQSY RGAQIFEAIG ISDAVINTYF PGTATQIGGI
PLKIIAQEAW LRHREAFHDI GYQSFTLDTG GEYQWRSNGE YHVYNPLAIH SLQQATRENN
RETYDLYADL MQNQNSAFLR GLLTFKSDRK PIPIEEVEPA EAIFKRFKTG AMSYGSISQE
AHEALAIAMN RIGGKSNSGE GGENPERFVK DENGDWRRSA IKQIASGRFG VTSHYLVNAE
ELQIKMAQGA KPGEGGHLPG QKVYPWISKT RGSTTGVGLI SPPPHHDIYS IEDLSQLIFD
LKNANHEARI NVKLVSKTGI GTIAAGVAKG LADVILVSGY EGGTGAAART SIRHAGLPWE
IGLAEAHQTL LLNGLRNQVV VETDGKLMTG KDVLVAAMLG AEEFGFATAP LVTLGCVMMR
VCHMDTCPVG VATQNPELRK KFGGSPDYVV NFFQFVVQEM REMMAEMGVR SLEELIGHKE
YLTTHERKDS HWKAKYIDFS KMLYQDDFYK NQIQYCTKPQ NHKIDQTLDM RELVPLIQPA
LETQAKVTGT FAVRNIDRAI GTIAGSYVSK KFGAVGLPED TIELDFIGSA GQSFGAYAPR
GMTLRVHGDA NDYLGKGLSG GKLIVSPQKE TPIDPHESAI AGNVTFYGAT GGEAYLHGKA
GARFAVRNSG AKVVVEGIGD NGCEYMTGGV AVILGEIGNN FAAGMSGGEA FIYAPERERF
VIKTNHEMVR IRSVEKNREI RLLKELIENH YRYTKSNFAK QLLANWEAEL KNFAYVIPNE
FELMRDRIET LEAEGNEHDA AELQAFYEHK DGKLLTGAGK
//