PYRK_BACSU
ID PYRK_BACSU Reviewed; 256 AA.
AC P25983;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit;
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit;
GN Name=pyrK; Synonyms=pyrDB, pyrDII, pyrZ, ylxD; OrderedLocusNames=BSU15530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1709162; DOI=10.1016/s0021-9258(18)31559-x;
RA Quinn C.L., Stephenson B.T., Switzer R.L.;
RT "Functional organization and nucleotide sequence of the Bacillus subtilis
RT pyrimidine biosynthetic operon.";
RL J. Biol. Chem. 266:9113-9127(1991).
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 FUNCTION.
RC STRAIN=168 / DB104;
RX PubMed=8759868; DOI=10.1128/jb.178.16.5013-5016.1996;
RA Kahler A.E., Switzer R.L.;
RT "Identification of a novel gene of pyrimidine nucleotide biosynthesis,
RT pyrDII, that is required for dihydroorotate dehydrogenase activity in
RT Bacillus subtilis.";
RL J. Bacteriol. 178:5013-5016(1996).
RN [4]
RP FUNCTION, COFACTOR, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-220; CYS-225; CYS-228; CYS-230 AND CYS-243.
RX PubMed=10545205; DOI=10.1006/abbi.1999.1455;
RA Kahler A.E., Nielsen F.S., Switzer R.L.;
RT "Biochemical characterization of the heteromeric Bacillus subtilis
RT dihydroorotate dehydrogenase and its isolated subunits.";
RL Arch. Biochem. Biophys. 371:191-201(1999).
CC -!- FUNCTION: Responsible for channeling the electrons from the oxidation
CC of dihydroorotate from the FMN redox center in the PyrD subunit to the
CC ultimate electron acceptor NAD(+). {ECO:0000269|PubMed:10545205,
CC ECO:0000269|PubMed:8759868}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10545205};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:10545205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10545205};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10545205};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000269|PubMed:10545205}.
CC -!- DISRUPTION PHENOTYPE: Decreased growth rate in pyrimidine-free medium,
CC extreme derepression of the pyrimidine biosynthetic operon, and
CC decreased, but detectable dihydroorotate dehydrogenase activity.
CC {ECO:0000269|PubMed:10545205}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M59757; AAA21271.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13427.1; -; Genomic_DNA.
DR PIR; G39845; G39845.
DR RefSeq; NP_389436.1; NC_000964.3.
DR RefSeq; WP_003232111.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P25983; -.
DR SMR; P25983; -.
DR STRING; 224308.BSU15530; -.
DR PaxDb; P25983; -.
DR PRIDE; P25983; -.
DR EnsemblBacteria; CAB13427; CAB13427; BSU_15530.
DR GeneID; 936854; -.
DR KEGG; bsu:BSU15530; -.
DR PATRIC; fig|224308.179.peg.1692; -.
DR eggNOG; COG0543; Bacteria.
DR InParanoid; P25983; -.
DR OMA; RYMKCGI; -.
DR PhylomeDB; P25983; -.
DR BioCyc; BSUB:BSU15530-MON; -.
DR BioCyc; MetaCyc:BSU15530-MON; -.
DR SABIO-RK; P25983; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.10.240.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01211; DHODB_Fe_S_bind; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR037117; Dihydroorotate_DH_ele_sf.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR023455; Dihydroorotate_DHASE_ETsu.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Pyrimidine biosynthesis; Reference proteome; Transport.
FT CHAIN 1..256
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit"
FT /id="PRO_0000148357"
FT DOMAIN 1..101
FT /note="FAD-binding FR-type"
FT BINDING 52..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 69..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 76..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 228
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 243
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT MUTAGEN 220
FT /note="C->A: No iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:10545205"
FT MUTAGEN 225
FT /note="C->A: No iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:10545205"
FT MUTAGEN 228
FT /note="C->A: No iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:10545205"
FT MUTAGEN 230
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:10545205"
FT MUTAGEN 243
FT /note="C->A: No iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:10545205"
SQ SEQUENCE 256 AA; 28099 MW; DC7B7605E39C2E15 CRC64;
MKKAYLTVCS NQQIADRVFQ MVLKGELVQG FTTPGQFLHL KVSEAVTPLL RRPISIADVN
FEKNEVTIIY RVDGEGTRLL SLKQQGELVD VLGPLGNGFP VNEVQPGKTA LLVGGGVGVP
PLQELSKRLI EKGVNVIHVL GFQSAKDVFY EEECRQYGDT YVATADGSYG ETGFVTDVIK
RKKLEFDILL SCGPTPMLKA LKQEYAHKEV YLSMEERMGC GIGACFACVC HTNESETSYV
KVCLDGPVFK AQEVAL
