GenomeNet

Database: UniProt
Entry: D7UU74_LISGR
LinkDB: D7UU74_LISGR
Original site: D7UU74_LISGR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system