PYRK_BACVZ
ID PYRK_BACVZ Reviewed; 256 AA.
AC A7Z4H3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
GN Name=pyrK {ECO:0000255|HAMAP-Rule:MF_01211}; OrderedLocusNames=RBAM_015360;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
CC -!- FUNCTION: Responsible for channeling the electrons from the oxidation
CC of dihydroorotate from the FMN redox center in the PyrD type B subunit
CC to the ultimate electron acceptor NAD(+). {ECO:0000255|HAMAP-
CC Rule:MF_01211}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01211};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01211};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01211}.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01211}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000255|HAMAP-
CC Rule:MF_01211}.
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DR EMBL; CP000560; ABS73899.1; -; Genomic_DNA.
DR RefSeq; WP_012117518.1; NC_009725.2.
DR AlphaFoldDB; A7Z4H3; -.
DR SMR; A7Z4H3; -.
DR STRING; 326423.RBAM_015360; -.
DR EnsemblBacteria; ABS73899; ABS73899; RBAM_015360.
DR KEGG; bay:RBAM_015360; -.
DR HOGENOM; CLU_003827_1_2_9; -.
DR OMA; RYMKCGI; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000001120; 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 3: Inferred from homology;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Pyrimidine biosynthesis; Transport.
FT CHAIN 1..256
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit"
FT /id="PRO_1000066394"
FT DOMAIN 1..101
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 52..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 69..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 76..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 220
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 228
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 243
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
SQ SEQUENCE 256 AA; 27896 MW; 8CEF388B92A00C2E CRC64;
MKKAHLTVQS NSEIADRIYK MVLKGELVRH LTEPGQFLHL KVSDAVTPLL RRPLSIADVN
FAADEVSVIY RADGEGTRLL AGKKEGGRID VLGPLGNGFP VRRIEPGKTA LLVGGGVGVP
PLQELSKRLT EKGVNVIHVL GFQSAKDVFY EQECRAYGDT YVATADGTYG EKGFVTDVIR
EKQLEFDVLL SCGPTPMLKA LKQQYGHKEV YLSMEERMGC GIGACFACVC RTGESDTSYV
KVCLDGPVFK AEEVAL
