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Database: UniProt
Entry: B1YIR8_EXIS2
LinkDB: B1YIR8_EXIS2
Original site: B1YIR8_EXIS2 
ID   B1YIR8_EXIS2            Unreviewed;       243 AA.
AC   B1YIR8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000256|HAMAP-Rule:MF_01211};
DE   AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000256|HAMAP-Rule:MF_01211};
GN   Name=pyrK {ECO:0000256|HAMAP-Rule:MF_01211};
GN   OrderedLocusNames=Exig_1942 {ECO:0000313|EMBL:ACB61394.1};
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB61394.1, ECO:0000313|Proteomes:UP000001681};
RN   [1] {ECO:0000313|EMBL:ACB61394.1, ECO:0000313|Proteomes:UP000001681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC   {ECO:0000313|Proteomes:UP000001681};
RX   PubMed=16489412; DOI=10.1007/s00792-005-0497-5;
RA   Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D.,
RA   Thomashow M.F., Tiedje J.M.;
RT   "Characterization of Exiguobacterium isolates from the Siberian permafrost.
RT   Description of Exiguobacterium sibiricum sp. nov.";
RL   Extremophiles 10:285-294(2006).
RN   [2] {ECO:0000313|EMBL:ACB61394.1, ECO:0000313|Proteomes:UP000001681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC   {ECO:0000313|Proteomes:UP000001681};
RX   PubMed=19019206; DOI=10.1186/1471-2164-9-547;
RA   Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.;
RT   "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain
RT   isolated from 3 million year old permafrost: a genome and transcriptome
RT   approach.";
RL   BMC Genomics 9:547-547(2008).
RN   [3] {ECO:0000313|Proteomes:UP000001681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC   {ECO:0000313|Proteomes:UP000001681};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_01211}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01211,
CC         ECO:0000256|PIRSR:PIRSR006816-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01211,
CC       ECO:0000256|PIRSR:PIRSR006816-1};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01211};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01211};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01211}.
CC   -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01211}.
CC   -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000256|ARBA:ARBA00006422,
CC       ECO:0000256|HAMAP-Rule:MF_01211}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01211}.
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DR   EMBL; CP001022; ACB61394.1; -; Genomic_DNA.
DR   RefSeq; WP_012370812.1; NC_010556.1.
DR   AlphaFoldDB; B1YIR8; -.
DR   SMR; B1YIR8; -.
DR   STRING; 262543.Exig_1942; -.
DR   KEGG; esi:Exig_1942; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_1_2_9; -.
DR   OMA; RYMKCGI; -.
DR   OrthoDB; 9778346at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000001681; 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   CDD; cd06218; DHOD_e_trans; 1.
DR   Gene3D; 2.10.240.10; Dihydroorotate dehydrogenase, electron transfer subunit; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR   PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01211};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01211};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01211};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01211};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01211, ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01211,
KW   ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01211,
KW   ECO:0000256|PIRSR:PIRSR006816-2};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01211}; Reference proteome {ECO:0000313|Proteomes:UP000001681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01211}.
FT   DOMAIN          1..93
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         46..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         68..69
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         209
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         214
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         217
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         230
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01211,
FT                   ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   243 AA;  26221 MW;  595206C73AC5B3C0 CRC64;
     MIQLLTVVSR REIAKGATEL ICRRPDATAI EPGRFMHLRV GPLLRRPISI ANVEGDLITF
     LFKEIGQGTK ELARLRAGDQ IDALGPLGNG FPVEHVAREA KIVLVGGGIG VPPLYYTMRR
     LVERGIACEA ILGFDTADSV FYEAEFQKLG PTTVTTVDGT AGIAGFVTAA LDSSRFDTLF
     ACGPEPMLRS IQQVPVEHKF LSIENRMGCG IGACFACVCP TPDGHYVKTC SDGPVFRAEE
     VIL
//
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