ID K2L232_9GAMM Unreviewed; 1489 AA.
AC K2L232;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:EKE83905.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:EKE83905.1};
GN Name=gltB {ECO:0000313|EMBL:EKE83905.1};
GN ORFNames=A10D4_07156 {ECO:0000313|EMBL:EKE83905.1};
OS Idiomarina xiamenensis 10-D-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE83905.1, ECO:0000313|Proteomes:UP000014115};
RN [1] {ECO:0000313|EMBL:EKE83905.1, ECO:0000313|Proteomes:UP000014115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-D-4 {ECO:0000313|EMBL:EKE83905.1,
RC ECO:0000313|Proteomes:UP000014115};
RX PubMed=23209204; DOI=10.1128/JB.01855-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL J. Bacteriol. 194:6938-6938(2012).
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:EKE83905.1}.
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DR EMBL; AMRG01000007; EKE83905.1; -; Genomic_DNA.
DR RefSeq; WP_008488627.1; NZ_AMRG01000007.1.
DR STRING; 740709.A10D4_07156; -.
DR PATRIC; fig|740709.3.peg.1455; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000014115; 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:EKE83905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014115}.
FT DOMAIN 13..403
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 887..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1489 AA; 163819 MW; B80D3A910EE93323 CRC64;
MSLYQHSDVR DNCGFGLIAN IHGETSHGLI KTAVTALDRM QHRGGISADG KTGDGCGLLL
QLPDSYFRYL AEQQQWQLGK KYAVGMIFLS HDPQRQQRAI DEIERQLAQE TLTLVGWREV
PTNADVLGDI ATQTQPVIRQ VFVSAQPGWR KKDIERRLYM ARRRIEQALS DDDDFYICSL
SCLVVVYKGL MMAGDLPAYY PDLADLRMET AICVFHQRFS TNTHPRWPLA QPFRYLAHNG
EINTIRGNRQ WAQARAYKMS SPLLPDLQQA RPFVNAQGSD SSALDNMLEL LLAGGMDLFR
AMRLLIPPAW QGDPTMGDDM RAFYEFNSMH MEPWDGPAGI VMSNGRHVAC CLDRNGLRPA
RYVLSKQGVL TVASEVGIWD YGEHDVLEKG RLGPGQMLAV DTYNGRIWRS HEIDQDLQQR
HPYRQWLNQH VRHLTPFSQC EAGQIGQRLF DDPQMKVFHK LFRYSEEELQ QVLAVLAKDG
QEAVGSMGDD TPLAVLSQHP RLLYDYFRQL FAQVTNPPID PIRERHVMSL ATCIGREQNV
FNETSGYAER VVLDSPILMY TDMQQLRQLE HEHYASTTLS LLYDPQQIDL QGAVIKLVEQ
AVEAVKAQRA VLLILSDRGI SQGLLPIAAP LAVGAVQQRL VRDSLRCDSN IIVETASARD
PHQFAVLIGL GATAVYPFLA YETIEQLVRQ QYVDRPMRDA LSAYREGINK GLLKIMSKMG
IATVASYRGS SLFEVIGLND EVCELCFATL ARRVNGAGFS DLQQDSLRVA RQAWLKRRPL
VQGGLLKYVH GGEYHAYNPD VVTSLQQAVI SNDKDAYQRF ANHVNQRPIA HLRDLLKLTP
VPTEQRPKLD NVESASHLMQ RFDSAAMSIG ALSPEAHEAL AQAMNRIGGH SNSGEGGEDP
KRFGSDRNSR IKQVASGRFG VTPHYLVNAD VIQIKVAQGA KPGEGGQLPG EKVTAEIAQL
RYAVAGTTLI SPPPHHDIYS IEDLAQLIFD LKQVSPKALV SVKLVSAPGI GTIAAGVAKA
YADLITVSGY DGGTGASPLS SVKHAGSPWE LGLAEVHQAL VENQLRHKVR VQVDGGLKTG
LDVIKAAILG AESFGFGTAP MVALGCKYLR ICHLNNCATG VATQDENLRR HHFSGLPERV
INYFQFVAEE VREWLQQLGV TELTQLIGRS DLLERIAGDT QRQQQIDLQP LLEAAATASP
LAKYCVESNP PYDRGQLNQQ LLARCCSAVD KRAGGDWQLS IRNDDRSVGA ALSGYVASRY
GNQGMATTPL KLRFSGSAGQ SFGAWNAGGV HLLLTGDAND YVGKGMAGGL LVLKPQAGVA
YASHQAIIMG NTCLYGATGG RLFAAGCAGE RFAVRNSGAT AVVEGIGDHG CEYMTGGVVA
ILGATGINFG AGMTGGFAYV LDEDGKMSER LNPALVQLEP VQGEVMKEHL RGLINDHYEA
TQSQRAQAML ADFEQYLRQF VLIKPKAADM RDLLGHRARS TAELRIQVM
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