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Database: UniProt
Entry: Q8YB40_BRUME
LinkDB: Q8YB40_BRUME
Original site: Q8YB40_BRUME 
ID   Q8YB40_BRUME            Unreviewed;       429 AA.
AC   Q8YB40; D0B621;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   OrderedLocusNames=BMEII1061 {ECO:0000313|EMBL:AAL54303.1};
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL54303.1, ECO:0000313|Proteomes:UP000000419};
RN   [1] {ECO:0000313|EMBL:AAL54303.1, ECO:0000313|Proteomes:UP000000419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094
RC   {ECO:0000313|Proteomes:UP000000419};
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA   Haselkorn R., Kyrpides N., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC       glycolate to glyoxylate. {ECO:0000256|PIRNR:PIRNR000139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC         ChEBI:CHEBI:17499; Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655; EC=1.1.99.14;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000139};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000256|PIRNR:PIRNR000139};
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DR   EMBL; AE008918; AAL54303.1; -; Genomic_DNA.
DR   PIR; AD3642; AD3642.
DR   RefSeq; WP_004686840.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YB40; -.
DR   GeneID; 29595487; -.
DR   KEGG; bme:BMEII1061; -.
DR   KEGG; bmel:DK63_2197; -.
DR   PATRIC; fig|224914.52.peg.2301; -.
DR   eggNOG; COG0247; Bacteria.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR012257; Glc_ox_4Fe-4S.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR32479; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR32479:SF17; GLYCOLATE OXIDASE IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13183; Fer4_8; 1.
DR   PIRSF; PIRSF000139; Glc_ox_4Fe-4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000139};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000139};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000139};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR000139};
KW   Membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000139};
KW   Oxidoreductase {ECO:0000313|EMBL:AAL54303.1};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
SQ   SEQUENCE   429 AA;  46785 MW;  D642E5B32DE625D4 CRC64;
     MQTHFSPEQL RDPGVLEAEK ILRKCVHCGF CTATCPTYVT LGNELDSPRG RIYLIKDMLE
     NGRPADEEIV RHVDRCLSCL ACMTTCPSGV NYMHLVDHAR AHIEKTYKRP FMNRLLRSVL
     AQVLPYPARF RLALKLAKLG KPFASLFRKS PVLRPVAAML DLAPQSLPAM PAATNAVRGE
     KRGRVAILNG CAQPVLNPGI NAATLRLLNR FDIEVATPKG EGCCGSLVHH MGREEQARHN
     VDVWTREIET GGLDAIIVTA SGCGTTIKDY GYMLRLDPAY KDKAARVSAL AKDITEYLAT
     LELPEPDAPK TLTVAYHSAC SMQHGQKIVR EPKDLLVKAG FTVKEPLEGH LCCGSAGTYN
     IMQPEIATKL RDRKVKNIEA TGAALIATGN IGCMTQIATG SDLPIVHTVE LIDWAYGGPT
     PQALEKAGA
//
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