PYRK_LACLA
ID PYRK_LACLA Reviewed; 262 AA.
AC Q9CFW7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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}; Synonyms=pyrZ;
GN OrderedLocusNames=LL1347; ORFNames=L183563;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK05445.1; -; Genomic_DNA.
DR PIR; C86793; C86793.
DR RefSeq; NP_267503.1; NC_002662.1.
DR RefSeq; WP_003131096.1; NC_002662.1.
DR PDB; 5KSW; X-ray; 2.47 A; B/D=1-262.
DR PDB; 5UE9; X-ray; 2.72 A; B/D=1-262.
DR PDBsum; 5KSW; -.
DR PDBsum; 5UE9; -.
DR AlphaFoldDB; Q9CFW7; -.
DR SMR; Q9CFW7; -.
DR STRING; 272623.L183563; -.
DR PaxDb; Q9CFW7; -.
DR EnsemblBacteria; AAK05445; AAK05445; L183563.
DR KEGG; lla:L183563; -.
DR PATRIC; fig|272623.7.peg.1453; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_9; -.
DR OMA; RYMKCGI; -.
DR BioCyc; MetaCyc:MON-14472; -.
DR SABIO-RK; Q9CFW7; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000002196; 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; 3D-structure; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Transport.
FT CHAIN 1..262
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit"
FT /id="PRO_0000148362"
FT DOMAIN 3..104
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 53..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 70..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 79..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 226
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 231
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 234
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 249
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT STRAND 5..17
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5KSW"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:5KSW"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5KSW"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:5KSW"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5KSW"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5KSW"
SQ SEQUENCE 262 AA; 28832 MW; D7AA45466E2C7FF1 CRC64;
MPKLQEMMTI VSQREVASNI FEMVLKGELV EEMDLPGQFL HLAVPNASML LRRPISISSW
DKVAKTCTIL YRIGDETSGT YEISKLQSGA KIDVMGPLGN GFPVDEVVST DKILIVGGGI
GVPPLYELAK QLEEKNCQMT ILLGFASEKV KILEKEFAEL KNVSLKIATD DGSYGTKGHV
GMLMEEIDFE VDALYTCGAP AMLKAVAKKY EQLERLYISM ESRMACGIGA CYACVEHDKE
DENHALKVCE DGPVFLGKQL LL
