ID A0A0C9N2A7_SPHPI Unreviewed; 1506 AA.
AC A0A0C9N2A7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GltB protein {ECO:0000313|EMBL:GAN13664.1};
GN Name=gltB {ECO:0000313|EMBL:GAN13664.1};
GN ORFNames=SP6_23_00640 {ECO:0000313|EMBL:GAN13664.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN13664.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN13664.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN13664.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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:GAN13664.1}.
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DR EMBL; BBJS01000023; GAN13664.1; -; Genomic_DNA.
DR RefSeq; WP_007406558.1; NZ_BBJS01000023.1.
DR SMR; A0A0C9N2A7; -.
DR GeneID; 78527322; -.
DR Proteomes; UP000032025; 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 25..422
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1506 AA; 163631 MW; E5142E0FDDDF085E CRC64;
MTFETEKQRL AEHGMYRPEF EGDACGVGMV AATDGQPSRR VVQSAIDALK AVWHRGAVDA
DGKTGDGAGL HVDLPHRFFD DAIAASGHKV LPNRLAVGMI FMPRTDLGAQ ETCRTIVESV
IIEAGYTIYG WRQVPVDVSV IGMKAQATRP EIEQIMIAGP MPDEVDAAEF EKNLYLIRRR
IEKRVIAAQI SGFYICSLSC RSIIYKGLFL AESLSVFYPD LQDHRFESRV AIFHQRYSTN
TFPQWWLAQP FRCLAHNGEI NTIRGNKNWM LSHEIRMASI AFGDNSEDIK PVIPAGASDT
AALDAVFEAI CRSGRDAPTA KLMLVPEAWQ KDLDTPKAHA EMYQYLASVM EPWDGPAALA
MTDGRWAVAG MDRNALRPLR YTLTADGLLI VGSESGMVVV PEATITAKGR LGPGQMIAVD
LAEGKLYDDR AIKDQIAGEQ DYAAMIGEFL TMDQLPQPSE GEALVRMPRA EMLRRQVAAG
QTMEDMELIL SPMAEGGKEA IGSMGDDTPL AVISDKPRLI SQFFRQNFSQ VTNPPIDSLR
ERYVMSLKTR FGNLANILDT EDRRERVLVL PSPVLTGADW HRLKAHFGRS AAEIDCTFEA
DGGPDRLRAA IQRIRNQAEQ AVREGRSELF LTDEHVGEDR VAIAGVLAAA AVHTHLVRRG
LRSYASINVR SAECLDTHYY AVLIGVGATT VNAYLAEAAI VDRHQRGLFG DLSIDQCLAN
HRTAIEDGLL KIMAKMGIAV ISSYRGGYNF EAVGLSRALV NDLFPGMPAK ISGEGYNSLH
YSAMVRHEAA WDQHVATLPI GGFYRQRDGG ETHAYSAQLM HLLQTAVATD SYSTYLQFAR
GVGDLPPVYL RDLLQFNFPN EGVPVDQVEA ITEIRKRFVT PGMSLGALSP EAHETLAIAM
NRIGAKAVSG EGGEDKLRYQ PYDNGDNANS TIKQIASGRF GVTAEYLNAC DEIEIKVAQG
AKPGEGGQLP GFKVTEFIAK LRHATPGVTL ISPPPHHDIY SIEDLAQLIY DCKQINPRAR
VCVKLVSSAG IGTVAAGVAK AHADVILVSG HVGGTGASPQ TSIKYAGTPW EMGLSEVNQT
LTLNGLRGRI RLRADGGLKT GRDIVIAAIL GAEEFGIGTL SLVAMGCIMV RQCHSNTCPV
GVCVQDERLR AKFTGTPEKV INLMTFIAEE VRDILARLGV RSLDEVIGRT ELLRQVSRGA
EHLDDLDLNP VLAKVDATDA ERRFSLSTFR NEVPDSLDAQ IIKDASAVFS RGEKMQLTYS
VRNTHRAVGT RLSSEITRKF GMSKLADGHV TVRLRGSAGQ SLGAFLCKGV TLEVFGDAND
YVGKGLSGGT IIVRPAVSSP LASQKNTIIG NTVLYGATSG KLFAAGQAGE RFAVRNSGAT
VVVEGCGANG CEYMTGGTAV VLGEVGANFG AGMTGGMAFI YDPEERFARR ANPENIVWQR
LASAHWEGVL RGLIEEHAAR TDSKWSKGLL EDWDRVAGHF WQVCPKEMLT RLAHPLDDSV
AAVAAE
//
