ID A0A164CKB9_9SYNE Unreviewed; 334 AA.
AC A0A164CKB9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glucose-6-phosphate 3-dehydrogenase {ECO:0000313|EMBL:KZR90502.1};
DE EC=1.1.1.361 {ECO:0000313|EMBL:KZR90502.1};
GN Name=ntdC {ECO:0000313|EMBL:KZR90502.1};
GN ORFNames=MITS9508_00502 {ECO:0000313|EMBL:KZR90502.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR90502.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR90502.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR90502.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:KZR90502.1}.
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DR EMBL; LVHU01000002; KZR90502.1; -; Genomic_DNA.
DR RefSeq; WP_067093188.1; NZ_LVHU01000002.1.
DR AlphaFoldDB; A0A164CKB9; -.
DR STRING; 1801629.MITS9508_00502; -.
DR PATRIC; fig|1801629.3.peg.551; -.
DR Proteomes; UP000076799; Unassembled WGS sequence.
DR GO; GO:0103074; F:glucose-6-phosphate 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43377; BILIVERDIN REDUCTASE A; 1.
DR PANTHER; PTHR43377:SF1; BILIVERDIN REDUCTASE A; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KZR90502.1}.
FT DOMAIN 8..124
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 159..323
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 334 AA; 36339 MW; CAC5008A44935C56 CRC64;
MTDAMVPVKV GVIGIGNMGW HHARVLSLLK DADLVGVADP DAQRGALATE QFGCRWFSDY
RTMLEEVEAV CIAVPTLLHH SVGLACLEAG SHVLIEKPIA ASQEEAAALI DAASRVGRLL
QVGHIERFNP AFRELTKVVA NEEVVVLEAR RHSPHADRAN DVSVVLDLMI HDLDLVLELA
SSSVVQLAAA GGRSSEGPID YVNATLGFEN GVVASLTASK MSHRKIRTLS AHCRASLVET
DFLNHNLHIH RRAHEWYSAD HGELLYRNDG FIEEVSTTSI EPLYAELEHF LQCVRGRETP
AVDGQQASRA LRLADLIEQA VEQPGVGVAI ETPI
//
