ID YGAK_BACSU Reviewed; 451 AA.
AC Q796Y5; P71091;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 4.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Uncharacterized FAD-linked oxidoreductase YgaK;
DE EC=1.-.-.-;
GN Name=ygaK; OrderedLocusNames=BSU08800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202460; DOI=10.1099/00221287-143-6-1855;
RA Cummings N.J., Connerton I.F.;
RT "The Bacillus subtilis 168 chromosome from sspE to katA.";
RL Microbiology 143:1855-1859(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 230.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB04812.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z82044; CAB04812.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12708.2; -; Genomic_DNA.
DR RefSeq; NP_388760.2; NC_000964.3.
DR RefSeq; WP_003233470.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q796Y5; -.
DR SMR; Q796Y5; -.
DR STRING; 224308.BSU08800; -.
DR PaxDb; 224308-BSU08800; -.
DR EnsemblBacteria; CAB12708; CAB12708; BSU_08800.
DR GeneID; 939245; -.
DR KEGG; bsu:BSU08800; -.
DR PATRIC; fig|224308.179.peg.950; -.
DR eggNOG; COG0277; Bacteria.
DR InParanoid; Q796Y5; -.
DR OrthoDB; 545125at2; -.
DR PhylomeDB; Q796Y5; -.
DR BioCyc; BSUB:BSU08800-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..451
FT /note="Uncharacterized FAD-linked oxidoreductase YgaK"
FT /id="PRO_0000360419"
FT DOMAIN 29..204
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 66
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000255"
FT CONFLICT 230
FT /note="A -> P (in Ref. 1; CAB04812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 50900 MW; 8F41028F1D598028 CRC64;
MEKTKLTGRI VTRDDPDYNE ARTNINLSLE RYPDIIVFCQ NKQDALNALK WARENRVPFR
IRGGRHSYEN FSLLNNGLVI DLSEMKKITV NQDKKLAYIE AGAELGEVYR TLWQYGLTLP
AGTIANVGLT GLTLGGGIGL LTRAAGLTCD SLVQLEMIVA DEKEGADLIT VSCSNHPDLF
WASQGGGGGN FGIVTSMTFK AVPISQVSIF SITWGWDDFE EVYNTWQNWA PYTDDRLTSS
IEFWPKEVNR IEALGQFVGP KTELKKLLKP LLKAGSPTSG MVKTTPFIEA VTFFNSPGGN
QPQKMKRSGS FIEKPLSERA ISTIKHFLEH APNQNASVWQ QALGGAAGRV APDQTAFYYR
DAIIAQEYLT NWTSPGEKRQ NVRWIEGLRT SLSKETMGDY VNWPDIEIRN WPRTYYGENV
ERLRRVKTTY DPENVFRFEQ SIPPLRRSLF F
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