ID A0A0A5GAI0_9BACI Unreviewed; 1517 AA.
AC A0A0A5GAI0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KGX90186.1};
GN ORFNames=N783_01455 {ECO:0000313|EMBL:KGX90186.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX90186.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX90186.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX90186.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX90186.1}.
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DR EMBL; AVPF01000009; KGX90186.1; -; Genomic_DNA.
DR RefSeq; WP_027446258.1; NZ_AVPF01000009.1.
DR STRING; 1385511.GCA_000425225_02569; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000030403; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030403}.
FT DOMAIN 22..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 891..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 168353 MW; 3B465D92A12116B3 CRC64;
MKYNQIPNSQ GLYHPELEHD ACGIGLYASI KGEATHDIVK KGLHMLCQLD HRGGQGSDPF
TGDGAGLLVQ IPDQFFQKTC TEMNLPSKGH YGVGMLFFSD DEERIAEEER INEVIEKEGQ
KVLGWRTVPI NVGKIGIGAQ KSCPIVRQVF VGASEDFQDE LAFERKLYVI RKQIEYWAKN
EGRDFYFPSF SSQTIVYKGL LLPEQVDAFY EDLQDEDFVS AFSLVHSRYS TNTFPSWERA
HPNRYIIHNG EINTLRGNIN WMRAREREMV SDAFGDDFKK LLPILDQSGS DSSVLDNAFE
FFVLAGRSPA HAAMMLIPEP WSQNENMSPE KKAFYEYHST LMEPWDGPTS ITFTDGKQIG
AILDRNGLRP ARYYVTKDDM IIYSSETGVI DVEEEDIVYK NRLSPGKMLL IDLEQERIIS
DDEVKSDVAQ AYPYQEWLDE NLVRLNEEDA EAESKSVPDV FTRQHAFGYT YEDIHKYLIP
MITEGKDPVG AMGNDAPLAV LSDRPQSLFN YFKQLFAQVT NPPIDSIREK LVTSTITYLG
AEGDILHPGE DNCHRLRIDS PVLSEGQFRQ IERDKYPEFK SRIIDALFVD DLEAELEEIC
EEAEKAIDDG VNLLVVSDRN MSETQVPVPT LLATSALHQH LVRERKRTEV SIIVESGEAR
EVHHFAALIG YGADAIYPYL AYETLAQTVE DDEALNISET EAVQKYRENV TTGIVKVMSK
MGISTIQSYR GAQIFEALGI SQKVIDRYFT GTVSQLDGID LDIIAKEAKE RHEVAYRDTF
NQTLESGSDF QWRKNGEFHA FNPTTIHKLQ WACRRNDYEL FKEYSEAANE ERMSFLRNLF
TFKEESPSIP IEEVESTDSI VQRFKTGAMS YGSLSQEAHE ALAIAMNRIG GKSNSGEGGE
DADRFKPDEN GDLRRSAIKQ IASGRFGVKS HYLVNAEELQ IKVAQGAKPG EGGQLPGKKV
YPWIGDVRGS TPGVGLISPP PHHDIYSIED LAQLIYDLKN SNRDARISVK LVAKSGIGTI
AAGVAKGAAD VIAVSGYDGG TGASPKTSIK HAGLPWELGL SETHQTLMLN GLRDRVTLET
DGKLMTGKDV VMASLLGAEE YGFATAPLVV LGCIMMRVCH KDTCPVGVAT QSPELRKKFT
GQADHIVNYM YFVAEEMREI MAELGFRTVE EMVGRTDVLD VSDRAKAHWK GKNLDLSKLI
YQPDGARTCQ KEQNHGIDQT LDVERILPKV SGAIKTKKPI KADFPIKNIN RTVGTIVGSE
ISKRYGEEGL PADTISLRFR GSAGQSFGAF VPKGLSLLLT GDANDYVGKG LSGGKIAVSK
PNDVPQSSDD VIIGNVAFYG ATDGEAYING RAGERFAVRN SGANVVVEGI GDHGCEYMTG
GRVVVLGDVG KNFAAGMSGG VAYVLTEDHE AFKSLCNQEL IDFEQLSDLE EITEVHSMIQ
AHWDHTGSLQ AGKLLSNWKE SVPKFVKVIP HDFKQMLQQI EAKRAGGLSD KEASLSAFQE
KFSKGKPSTN KPVLAGK
//
