ID E9T818_RHOHA Unreviewed; 1528 AA.
AC E9T818;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Class II glutamine amidotransferase {ECO:0000313|EMBL:EGD21422.1};
GN ORFNames=HMPREF0724_14924 {ECO:0000313|EMBL:EGD21422.1};
OS Prescottella equi ATCC 33707.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Prescottella.
OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD21422.1, ECO:0000313|Proteomes:UP000004245};
RN [1] {ECO:0000313|EMBL:EGD21422.1, ECO:0000313|Proteomes:UP000004245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD21422.1,
RC ECO:0000313|Proteomes:UP000004245};
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 (JAN-2011) 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:EGD21422.1}.
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DR EMBL; ADNW02000033; EGD21422.1; -; Genomic_DNA.
DR RefSeq; WP_005516535.1; NZ_CM001149.1.
DR STRING; 43767.A6I91_17020; -.
DR HOGENOM; CLU_000422_8_2_11; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000004245; 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: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:EGD21422.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000004245};
KW Transferase {ECO:0000313|EMBL:EGD21422.1}.
FT DOMAIN 20..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 914..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1528 AA; 165616 MW; ABDB3C149BDF647C CRC64;
MKHLPGPQGL YHPANEHDAC GVAFVVDMHG RRSRDIVEKA ITALVNLEHR GAAGSEPNTG
DGAGILLQVP DRFLRAVVDF ELPAAGAYAT GIAFLPQGDA AADEAAAGVE KIVAEEGLTV
LGWREVPTDD SSLGTLARAA MPTFRQVFIG SAGDSVTDMD LERRAYVIRK RVEHELGESG
AGEDGPGRES VYFPSLSGQT FVYKGMLTTP QLKGFYLDLQ DDRVESALGL VHSRFSTNTF
PSWPLAHPFR RVAHNGEINT VSGNENWMRA REALIKSDVF GDGALEKIFP ICTPGASDTA
RFDEVLELLH LGGRSLPHAV LMMIPEAWER HESMDPARKA FYEYHSALME PWDGPASVCF
TDGTVVGAVL DRNGLRPSRV WVTDDGLVVM ASEVGVLDIA PEKIVRRMRM QPGRMFLVDT
AQGRIISDDE IKSELAAEHP YQQWIDEGLV QIDDLPESKY TYMTHDRVVL RQQIFGFTNE
EVNLLVKPMA VTGGEALGSM GTDTPIAVLS ARPRMLFDYF QQLFAQVTNP PLDAIREEIV
TSLGGTIGPE ADLLTPSAAS CRQIVLPQPI LHNDDLSKLI HLNDNAKFPH FRSVVVRGVY
PVAQGGEGLR KALDTVRDKV SEAIAGGARI IVLSDRESNE KYAPIPSLLL TAAVHHHLVR
EKTRTKVGLV VESGDAREVH HMAALLGFGA SAVNPYMAFE TIDELLQSDQ LAGLSLDKAV
TNYIKAAGKG VLKVMSKMGI STLASYTGAQ LFQVIGLSQE LVDEYFTGLQ SNLDGIGLDE
IAADVAARHA NAYLDRPELR AHRELEVGGE YQWRREGEYH LFNPDTVFKL QHSTKTGQYE
VFKEYTKLVD DQSERLASLR GLFKFKSGLR QPISIDEVEP ASEIVKRFST GAMSYGSISA
EAHETLAIAM NRLGGRSNSG EGGEHPSRFT PDENGDWRRS AIKQVASGRF GVTSHYLSNC
TDIQIKMAQG AKPGEGGQLP PHKVYPWVAE VRGSTPGVGL ISPPPHHDIY SIEDLAQLIH
DLKNANPQAR IHVKLVSEIG VGTVAAGVSK AHADVVLISG HDGGTGASPL TSLKHAGAPW
ELGLAETQQT LLLNGLRDRI VVQVDGQMKT GRDVMIATLL GGEEFGFATA PLVVSGCIMM
RVCHLDTCPV GVATQNPVLR KRFAGKPEFV ENFFMFIAEE VRELLAELGF RTLQEAVGQV
DVLDTTAALE HWKASKLDLS PILHRVESAF ADQDLYCSGT QEHGLEKALD QQLIQLARPA
LDKGEAVAFE SEITNVNRTV GTMLGHEVTK AYGAEGLPDN TIDITFTGSA GNSFGAFVPK
GMTLRLHGDA NDFVGKGLSG GRIVVRPPLK TAEGFVPEDN IIGGNVLLFG ATAGEALVRG
IVGERFAVRN SGATAVVEGV GDHACEYMTG GKVVILGKTG RNFGAGMSGG VAFIFNPDRD
FGTNLNTELV DLEDLSVEDL EWLHGAVERH RDETGSEVAA RILADWSHQK AHFAKVMPRD
YKKVLVAIET AKKNGTNVDD AIMEAARG
//
