ID A0A1U7MCW1_9FIRM Unreviewed; 433 AA.
AC A0A1U7MCW1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=lutA_5 {ECO:0000313|EMBL:OLS55373.1};
GN ORFNames=SPSPH_34210 {ECO:0000313|EMBL:OLS55373.1};
OS Sporomusa sphaeroides DSM 2875.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS55373.1, ECO:0000313|Proteomes:UP000186950};
RN [1] {ECO:0000313|EMBL:OLS55373.1, ECO:0000313|Proteomes:UP000186950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS55373.1,
RC ECO:0000313|Proteomes:UP000186950};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL Submitted (FEB-2016) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLS55373.1}.
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DR EMBL; LSLJ01000004; OLS55373.1; -; Genomic_DNA.
DR RefSeq; WP_075757034.1; NZ_LSLJ01000004.1.
DR AlphaFoldDB; A0A1U7MCW1; -.
DR STRING; 1337886.SPSPH_34210; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000186950; Unassembled WGS sequence.
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; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186950};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 6..37
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 433 AA; 47298 MW; F609905524248488 CRC64;
MNKQERRQLI EQEIVKCSRC GNCRSICPVF LAENNENTTP RSKARLLEAV LENDIELTAG
VQQRFEKCLF CKACLTHCGS GVATDKVILA ARTAAAERNG ISPMKKLAFT GLRYRKLFDL
CLRAGALFQH VIFKKLPDGR GRAPRILLPG AGLNQRRIMP DMTVSPLRTR LPEFIPAKKA
DSQGTVLFFT GCMLNYFYPQ TGDAVVNILT ANGWNVVIPA EQCCCGTPAF TSGDEATGRV
LAEQNVQAIG SKKYDHIVTA CASCGAALKE EYAHILGDSP LLAASQNVAG KVLDITQFVL
QHCDLTKLGK VPLKVTYHDP CHLVRGMQVS AEPRQILQSI PGLEYVEMKD ASRCCGAGGS
FSAVYYELSR HINDKKLDNA ANTGTDYCIT GCSSCRMHIT DGLTQRHSPM KVLHTAEIIS
MAYEAGGKEG ETC
//
