ID A0A0J1H757_9GAMM Unreviewed; 1487 AA.
AC A0A0J1H757;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KLV07568.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KLV07568.1};
GN Name=gltB {ECO:0000313|EMBL:KLV07568.1};
GN ORFNames=ABT57_16865 {ECO:0000313|EMBL:KLV07568.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV07568.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV07568.1, ECO:0000313|Proteomes:UP000035909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV07568.1,
RC ECO:0000313|Proteomes:UP000035909};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLV07568.1}.
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DR EMBL; LDOU01000016; KLV07568.1; -; Genomic_DNA.
DR RefSeq; WP_047886439.1; NZ_PYMI01000001.1.
DR STRING; 320778.ABT57_16865; -.
DR PATRIC; fig|320778.3.peg.3669; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000035909; 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: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 ECO:0000313|EMBL:KLV07568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035909}.
FT DOMAIN 13..403
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1487 AA; 162427 MW; D82A0F888E38CA1E CRC64;
MTLYDPTLDK DNCGFGLIAH IEGQTSHKLV RTAISALDRM THRGGIAADG KTGDGCGLLM
KKPDSFYRII AEEKGWKLSR EFALGMVFLS QDPVLAEQAR TIINEELAKE TLSLVGWREV
PINPKVLGPI ATENLPNIEQ VFVNAPAGWK PRDIDRRLYV ARRRIEKRIS SDPDFYICSL
STQVTVYKGL CMPADLPRFY KDLGDIRLES SICLFHQRFS TNTQPRWPLA QPFRYLAHNG
EINTIAGNRQ WARARAYKFA SPLLPDLQNA APFVNETGSD SSSLDNMLEL FLSGGMDLFR
AMRMLVPPAW QNHPDMDPEL RAFYDFNSMH MEPWDGPAGI VMSDGRYAAC NLDRNGLRPA
RYVITKDKLI TLASEVGIWD YAPDEVAEKG RVGPGELLVI DTKFGKIWHS DDIDNDLMER
HPYKEWMDSH VKRLVPFEDL GDDQVGSRSL SDNELSTYQK LFGISREELD QVIRVMGEIG
QEATGSMGDD APMAVLSSKE RAVTDYFRQM FAQVTNPPID PLREKHVMSL ATCIGREMNV
FCETDGHAYR VAFASPVLLY SDLVQLLELD DQHYRNSIID INFDPSEKDL KQAILDVCDQ
AERLVRNGTV LLVLSDRGVT PEKLPIPAAM AVGAVQNRLV AQNLRCDANI IVETAAARDP
HQFAVLLGFG ATAIYPYLAY ESLGKLADSG ALTHPYREVM LNFRNSINKG LYKIMSKMGI
STIASYRCSM LFEAVGLDSE VVDLCFKGVS SRIQGAGFSD FQQDLFNLSR RAWLKRKPIE
HGGLLKYVHG GEFHAYNPDV VGTLQKAVRS GDYQDYLAFA REVNERPVAA IRDLFKLKTS
GDPIALEQVE AATELFKRFD SAAMSIGALS PEAHEALAIA MNRLGGYSNS GEGGEDPRRF
NTERNSRIKQ VASGRFGVTP HYLVNADVLQ IKVAQGAKPG EGGQLPGHKV TTEIAKLRFA
VPGVTLISPP PHHDIYSIED LAQLIFDLKQ VNPDALVSVK LVSEPGVGTI ATGVAKAYAD
LITISGYDGG TGASPLTSVK YAGSPWELGL AETQQALVAN GLRHKIRLQV DGGLKTGLDV
VKAAILGAES FGFGTAPMVA LGCKYLRICH LNNCATGVAT QDETLRRDFF KGLPDQVMNY
FIGLGQEVRD LLATLGVEKL TDLIGRTDLL EVVEGYTAKQ SKLDLSPILA TAEPQPGKTL
YCSEPNTPFD PATLNAALLE QALPAIESRS GADIFQNIRN TDRSVGARLS GEIAKRWGNQ
GMAASPINLH LTGTAGQSFG VWNAGGLNLY LTGDANDYVG KGMAGGQIVI RPPVGSAFKS
SDATIVGNTC LYGATGGKLY AAGKAGERFG VRNSGAIAVI EGAGDNACEY MTGGIVAILG
KTGVNFGAGM TGGFAYILDE DGDFAGRVNP ELVEALPLAE LKIHQEHLRG LIDQHLEHTG
SSRAQEILAE FDQWIPKFYL AKPKSADVNT LLGHQSLSAA ELRVQAQ
//
