ID A0A329ZCP8_9HELI Unreviewed; 490 AA.
AC A0A329ZCP8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:RAX51570.1};
GN ORFNames=CCY99_08910 {ECO:0000313|EMBL:RAX51570.1};
OS Helicobacter sp. 16-1353.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004996 {ECO:0000313|EMBL:RAX51570.1, ECO:0000313|Proteomes:UP000251728};
RN [1] {ECO:0000313|EMBL:RAX51570.1, ECO:0000313|Proteomes:UP000251728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-1353 {ECO:0000313|EMBL:RAX51570.1,
RC ECO:0000313|Proteomes:UP000251728};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:RAX51570.1}.
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DR EMBL; NHYM01000018; RAX51570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZCP8; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000251728; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; 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; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
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; 2.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 23..138
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 154..471
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 490 AA; 54476 MW; E71A6FF7435116CF CRC64;
MGKITGFLDF KREDLGQRNY KERIKDYKTF YKPLNKDKRE IQASRCMNCG VPFCQVAINI
KGHSVGCPLG NLIPEWNDLL SKGFWAEAYE RLSKTSPFSE FTGSVCPAPC ENSCVCGANG
LPITIRDNEL SLISWAFESG YLKPKTNIKR NGKNIAVIGS GPAGLAVANR LNHLGYEVSI
FERSDRIGGL LMYGIPDMKL DKALIERRVT LMEKEGVRFY PNTNIATKQK ADELLKSFNA
VILATGASKP LDLEIPGRNL NGIMFAVDFL TQNTKSLLDT KKPLEVAKNK DVLVIGSGDT
SVDCIAVALR QGAKSITRFE RSAKKPLERE GDNLWPEYPN ILTTDYGIKE AIECLGYDPR
MYQKLTKNFV GDSANKNVKG LEAVDLKWEV QNGKKVRSEV PNSLKFYKAD LVLLAMGFAG
SEENTADIFK VKLDNKNNIA TNNYQTSNPK IFACGDARMG QSLVVWAIKE ALNCANALDL
HFKKQNLRAI
//
