ID D2Q313_KRIFD Unreviewed; 1512 AA.
AC D2Q313;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADB32138.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ADB32138.1};
GN OrderedLocusNames=Kfla_3074 {ECO:0000313|EMBL:ADB32138.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB32138.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB32138.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
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}.
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DR EMBL; CP001736; ADB32138.1; -; Genomic_DNA.
DR STRING; 479435.Kfla_3074; -.
DR MEROPS; C44.003; -.
DR KEGG; kfl:Kfla_3074; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) 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 InterPro; IPR001202; WW_dom.
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.
DR PROSITE; PS50020; WW_DOMAIN_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:ADB32138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT DOMAIN 27..414
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 315..350
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 907..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 163769 MW; 33AB8F541A6A205E CRC64;
MFGRPPILNR QRPAEGLYDG QHEHDACGVA FVATLTGEPS HDIVAKALTA LRNLEHRGAS
GAEPDSGDGA GILIQVPDAF YRKVCDFELP VARAYATGIA FLPQDPDDAA KAVARIEELA
DEENLTVLGW RDVPTTPDLL GATARSVMPV FRQLFVAAKT GRVLGLALER MAFRLRKRAE
RETATYFPSL SGRTVTYKGM LTTDQLDKFF PELTDPDLAS AIGVVHSRFS TNTFPSWPLA
HPYRYIAHNG EINTVQGNRN WMRAREALLA SDLIPGDLEQ LYPICTPGAS DSASFDEVLE
LLHLGGRSLP HAMLMMIPEA WENATTMDPK RRAFYEFHST LMEPWDGPAS VVFSDGTKVG
AVLDRNGLRP SRYWVTEDGL VVLASEAGVL DIDPATVTQK GRLEPGRIFL VDVEQHRIIT
DSEVKTALAE EHPYDEWLHA GLIRFEDLQE REHVVHSHAS VTRRQQVFGY TEEELRLLLT
PMAKTGAEPI GSMGTDTPIA VLSDRPRLLF DYFAQLFAQV TNPPLDAIRE ELVTSLSSSL
GPESNLLNPS PASCRQVVLP FPVITNDELA KLRHINLDGD MPGLATTVLR GVYDVAGGGQ
ALKDRLDAIC AEASAAIAEG ARILVLSDRH SNAEHAPIPS LLLTSAVHHH LVREKTRTQV
GLVIEAGDVR EVHHVALLMG YGAACINPYL ALESAEDLAR RGTYLPGIEP EQAVRNVVKS
LGKGVLKVMS KMGVSTVASY TGAQIFEATG LSADLVDTYF TGTSSKLGGV GLDVIAEEVR
QRHLRAYPAD GILPAHRKLE VGGEYQWRRE GEPHLFDPET VFRLQHSTRT GRYDIFKQYT
QRVDQQSEQL MTLRGLFAFR SDRQPISVDE VEPVSEIVKR FSTGAMSYGS ISAEAHETLA
VAMNRLGGKS NTGEGGENSD RLHDPARRSS IKQVASGRFG VTAEYLTNSD DIQIKMAQGA
KPGEGGQLPG HKVYPWVAST RHSTPGVGLI SPPPHHDIYS IEDLAQLIHD LKNANPSARI
HVKLVSEVGV GTIAAGVSKA HADVVLISGH DGGTGAAPLT SLKHAGGPWE LGLAETQQTL
LLNGLRDRIV VQTDGQLKTG RDVVVAALLG AEEYGFATAP LVVSGCIMMR VCHLDTCPVG
VATQNPVLRE RYAGKPEFVV NFFEFIAEEV REYLAELGFR SLDEAIGHAD VLDIQRAVDH
WKADGLDLSP ILHVPALPEG AARHQTVLQD HGLDKALDNE LIRICAPAIE NGEPVRAQLP
IRNVNRTVGT MLGHEITKKY RAAGLPDGTV DLTFTGSAGN SFAAFVPRGV TLRLEGDAND
YVGKGLSGGR VVIRPDRNAR FDAADQIIAG NVIAYGATSG ELFINGGAGQ RFCVRNSGAT
AVVEAVGDHA CEYMTGGRVV VIGAVGRNFA AGMSGGVAHV LDLDPALVNP ELVDLLPLTG
EESDLLQDLV RRHHEETGSE RAAKLLADWA AAETRFTTVM PRDYARVLAA KAAAERDGLD
EDATTRAMME AI
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