ID A0A0S7ZZ07_9GAMM Unreviewed; 600 AA.
AC A0A0S7ZZ07;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KPJ91532.1};
DE Flags: Fragment;
GN ORFNames=AMJ53_11495 {ECO:0000313|EMBL:KPJ91532.1};
OS Gammaproteobacteria bacterium SG8_11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703402 {ECO:0000313|EMBL:KPJ91532.1, ECO:0000313|Proteomes:UP000051175};
RN [1] {ECO:0000313|EMBL:KPJ91532.1, ECO:0000313|Proteomes:UP000051175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_11 {ECO:0000313|EMBL:KPJ91532.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ91532.1}.
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DR EMBL; LJNJ01000225; KPJ91532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7ZZ07; -.
DR Proteomes; UP000051175; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 30..135
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 148..461
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 600
FT /evidence="ECO:0000313|EMBL:KPJ91532.1"
SQ SEQUENCE 600 AA; 65498 MW; 71941AF2E27E0CC1 CRC64;
MATPADKVKQ AHTFRKFKDH ENPDAMPLKE KIFEADHSHK CPTYIHQTPP CQGSCPSGED
IRGWLNIVRG IEKPSGDMTW KEYAFRRSTD ANPFPAIMGR VCPAPCEDGC NRNEVEDHVG
INAVEQFIGD NALNEGYKFA PGKDTGKSVG IIGGGPCGLA AAYQLRRMGH GVTVYEAQQE
LGGMMMYGIP GYRTPREVLH GEMNRIVDMG VEVKTNTRVG KDISIAELEK KHDAVLFAIG
AQSGRLLPIP GGDKAPNCIS GVAFLEAFNQ GRLKAVSGKV VVVGGGDTSI DVVSVARRLG
NVTNIAEKDR PENIVLGHTA HDVADIANKE GADTTLISRH PIDGMTAAKH EIDDALREGV
KIQGSLNPVE VVLDDSGRAK ALRVAKLSYE SGKPEQIPGS EFDIEADLIV SAIGQTGDFT
GMEDFNNGKG LIDADKHFQV PNKPGFFVAG DIVRPHLLTT VIGQASVVAD TIDHYFKHKE
LAKRPKVDVH HFDLMSKLHE AGLDPEKFNP DGDAKIRGID RGLRGTNDAD FAIHNYEDRS
KHQIIPSDEL FLGHFKYEPR HKRQESVPDA EEVLGHFEER VMGLSEEETV AEAERCMSCG
//
