ID D4E1A3_SEROD Unreviewed; 1489 AA.
AC D4E1A3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Class II glutamine amidotransferase {ECO:0000313|EMBL:EFE96448.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:EFE96448.1};
GN Name=gltB {ECO:0000313|EMBL:EFE96448.1};
GN ORFNames=HMPREF0758_1877 {ECO:0000313|EMBL:EFE96448.1};
OS Serratia odorifera DSM 4582.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE96448.1, ECO:0000313|Proteomes:UP000005723};
RN [1] {ECO:0000313|EMBL:EFE96448.1, ECO:0000313|Proteomes:UP000005723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE96448.1,
RC ECO:0000313|Proteomes:UP000005723};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-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:EFE96448.1}.
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DR EMBL; ADBY01000032; EFE96448.1; -; Genomic_DNA.
DR RefSeq; WP_004958175.1; NZ_GG753567.1.
DR STRING; 667129.HMPREF0758_1877; -.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000005723; 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; 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 ECO:0000313|EMBL:EFE96448.1}; 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:EFE96448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005723};
KW Transferase {ECO:0000313|EMBL:EFE96448.1}.
FT DOMAIN 12..404
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1489 AA; 163426 MW; 99775E3FAE219FDE CRC64;
MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK TGDGCGLLLQ
KPDRFFRMVA EERGWRLAKN YAVGMMFLSQ DEEQARASRR IVEEELQNET LSIVGWREVP
TNPDVLGEIA LSSLPRIEQI FVNAPAGWRP RDMERRLFVA RRRIEKRVQE VQDDSFYVCS
FSNLVTIYKG LCMPADLPRF YLDLADLRLE SAICLFHQRF STNTVPRWPL AQPFRYLAHN
GEINTITGNR QWARARTYKF QTPLIPDLQS AAPFVNETGS DSSSLDNMLE LLLAGGMDLI
RAMRLLVPPA WQNNPDMDGD LRAFFDFNSM HMEPWDGPAG IVMSDGRYAA CNLDRNGLRP
ARYVITKDKL ITCASEVGIW DYQPDEVVEK GRVGPGELMV IDTRSGRILH SAETDNDLKS
RHPYKEWMEK NVKRLVPFED LPEDQVGSRE LDDATLETYQ KQFGYSSEEL DQVIRVLGEI
GQEATGSMGD DTPFAVLSSR PRIIYDYFRQ QFAQVTNPPI DPLREAHVMS LATSIGREMN
VFCEAEGQAH RLSFKSPILL YSDFKQLTTL EGEYYRADTL DLTFDPAEQD LEQKIRALCD
EAERKVRDGA VLLVLSDRAI APNRLPVPAP MAVGAVQTRL VEKSLRCDAN IIVETASARD
PHHFAVLLGF GATAIYPYLA YETLAKLVDS QAIDKKYRDV MLNYRNGINK GLYKIMSKMG
ISTVASYRCS KLFEAVGLHR DLSDLCFQGV VSRISGASFS DFQQDLQNLS KRAWLKRKPL
DQGGLLKFVH GGEYHAYNPD VVNTLQKAVH SGEYADYQAY AKLVNQRPVA MLRDLLAITP
KGAPIPVDQV EPAESLFGRF DTAAMSIGAL SPEAHESLAI AMNSLGGFSN SGEGGEDPAR
YRTNKVSRIK QVASGRFGVT PAYLVNADVI QIKVAQGAKP GEGGQLPGDK VTPYIAKLRY
SVPGVTLISP PPHHDIYSIE DLAQLIFDLK QVNPKAVISV KLVSEPGVGT IATGVAKAYA
DLITIAGYDG GTGASPLSSV KYAGCPWELG LVETQQALVA NGLRHKIRLQ VDGGLKTGVD
IVKAAILGAE SFGFGTGPMV ALGCKYLRIC HLNNCATGVA TQDEKLRRDH YHGLPERVTN
YFQFIARETR EIMASLGVSQ LVDLIGRTEF LTELDGISAK QNKLDLSPLL QTATPHPGKA
VYCTESSNPA FDRGLLNKEL LAQAEPFIEA KHSKTFYFDI RNTDRSVGAT LSGAIAAVHG
DQGMAADPIK AHFSGTAGQS FGVWNAGGVE LTLTGDANDY VGKGMAGGSI AVRPPVGSAF
RSFEASIIGN TCLYGATGGK LFAAGRAGER FAVRNSGAIT VVEGIGDNGC EYMTGGIVCV
LGKTGINFGA GMTGGFAYVL DEDGEFRKRV NPELVEVLDV DQLAIHEEHL RGLITEHVQA
TGSARAEEIL ANWPEWASKF ALVKPKSSDV KALLGHRSRS AAELRVQAQ
//
