ID E8WQY2_GEOS8 Unreviewed; 446 AA.
AC E8WQY2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN OrderedLocusNames=GM18_3793 {ECO:0000313|EMBL:ADW15219.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW15219.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW15219.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW15219.1,
RC ECO:0000313|Proteomes:UP000001442};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA Aklujkar M., Lovley D., Woyke T.;
RT "Complete sequence of Geobacter sp. M18.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002479; ADW15219.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WQY2; -.
DR STRING; 443143.GM18_3793; -.
DR KEGG; geb:GM18_3793; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_7; -.
DR Proteomes; UP000001442; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:SF20; 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; SSF46548; alpha-helical ferredoxin; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000139}; Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 30..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 81..110
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 446 AA; 48251 MW; 17FB51CD31A5C7B6 CRC64;
MIPRIPIAHI SPIALKREQS MSKKQVDPLE RVAQEMKKCV KCGACRANCP AFGTFQREPA
TARGKVALAQ HLVKGDITLD DGTYSAMSKC LLCGSCVDKC PNQVPTDEIV IAAREALAQR
RGLTSFHKAV GQVIKNRKLM NFGALAAAVL GPIFFRKVPT TSGLRLRFPM PFLGGSRHVP
QIAKKPFMKR HPEVIKGEPG KPTIVFFVGC MTNFVYTEIG EATLALFRHL GCTVIIPQGQ
QCCGLPGMSG GDLETVRELA EQNLAAIEKH QADYVMTACA TCGGALHKLY PLVIGKRNPE
LKARLQAVAD KTVDAAVLLQ KLGLHPEETG TGQRMRVTYH DPCHHRTAGI AKQPRTLLQQ
TPGLDLVEME GADRCCGLGG TFNVYHYESS LDINAGKSAA IIDTGADAVV TGCPGCIMQL
SDGLKQAGDK TKVLHTVELL ARKIKR
//
