ID Q7MAW0_PORGI Unreviewed; 313 AA.
AC Q7MAW0;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Enoyl-(Acyl-carrier-protein) reductase II {ECO:0000313|EMBL:AAQ66470.1};
GN Name=fabK {ECO:0000313|EMBL:AAQ66470.1};
GN OrderedLocusNames=PG_1416 {ECO:0000313|EMBL:AAQ66470.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66470.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66470.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2] {ECO:0007829|PDB:4IQL}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FMN AND NADPH.
RX PubMed=29400320; DOI=10.1107/S2053230X18000262;
RA Hevener K.E., Santarsiero B.D., Lee H., Jones J.A., Boci T., Truong K.,
RA Johnson M.E., Mehboob S.;
RT "Structural characterization of Porphyromonas gingivalis enoyl-ACP
RT reductase II (FabK).";
RL Acta Crystallogr. F 74:105-112(2018).
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DR EMBL; AE015924; AAQ66470.1; -; Genomic_DNA.
DR RefSeq; WP_005873413.1; NC_002950.2.
DR PDB; 4IQL; X-ray; 1.94 A; A/B=1-313.
DR PDBsum; 4IQL; -.
DR AlphaFoldDB; Q7MAW0; -.
DR SMR; Q7MAW0; -.
DR STRING; 242619.PG_1416; -.
DR EnsemblBacteria; AAQ66470; AAQ66470; PG_1416.
DR KEGG; pgi:PG_1416; -.
DR PATRIC; fig|242619.8.peg.1316; -.
DR eggNOG; COG2070; Bacteria.
DR HOGENOM; CLU_038732_1_1_10; -.
DR BioCyc; MetaCyc:HMPREF1322_RS00185-MONOMER; -.
DR BioCyc; PGIN242619:G1G02-1318-MONOMER; -.
DR BRENDA; 1.3.1.10; 756.
DR BRENDA; 1.3.1.39; 756.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR PANTHER; PTHR32332; 2-NITROPROPANE DIOXYGENASE; 1.
DR PANTHER; PTHR32332:SF20; 2-NITROPROPANE DIOXYGENASE-LIKE PROTEIN; 1.
DR Pfam; PF03060; NMO; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4IQL}; Flavoprotein {ECO:0007829|PDB:4IQL};
KW FMN {ECO:0007829|PDB:4IQL}; Nucleotide-binding {ECO:0007829|PDB:4IQL};
KW Reference proteome {ECO:0000313|Proteomes:UP000000588}.
FT DOMAIN 4..75
FT /note="Nitronate monooxygenase"
FT /evidence="ECO:0000259|Pfam:PF03060"
FT DOMAIN 80..300
FT /note="Nitronate monooxygenase"
FT /evidence="ECO:0000259|Pfam:PF03060"
FT BINDING 18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 25
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 26
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 44
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 46
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 49
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 52
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 53
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 75
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 94
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 190
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 192
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 193
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 202
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 260
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IQL"
FT BINDING 263
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4IQL"
SQ SEQUENCE 313 AA; 33087 MW; 9E3147BAA216D740 CRC64;
MNRICELLGI EHPIISGGMV WCSGWKLASA VSNCGGLGLI GAGSMHPDNL EHHIRSCKAA
TDKPFGVNVP LLYPEMDKIM EIIMREHVPV VVTSAGSPKV WTAKLKAAGS KVIHVVSSAT
FARKSEAAGV DAIVAEGFEA GGHNGREETT TLCLIPEVVD AVNIPVVAAG GIASGRAVAA
ALALGADAVQ VGTRFALSEE SSAHEDFKAH CRRSVEGDTM LSLKAVSPTR LLKNKFYQDV
FAAEQRGASV EELRELLGRG RAKQGIFEGD LHEGELEIGQ AVSQISHAET VAEIMVDLVD
GYKRSLAGMP TEI
//
