ID A0A1T4PFU0_9GAMM Unreviewed; 403 AA.
AC A0A1T4PFU0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=SAMN02745674_01181 {ECO:0000313|EMBL:SJZ90443.1};
OS Lysobacter spongiicola DSM 21749.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1122188 {ECO:0000313|EMBL:SJZ90443.1, ECO:0000313|Proteomes:UP000190061};
RN [1] {ECO:0000313|EMBL:SJZ90443.1, ECO:0000313|Proteomes:UP000190061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21749 {ECO:0000313|EMBL:SJZ90443.1,
RC ECO:0000313|Proteomes:UP000190061};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXP01000003; SJZ90443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4PFU0; -.
DR STRING; 1122188.SAMN02745674_01181; -.
DR OrthoDB; 9765258at2; -.
DR Proteomes; UP000190061; 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:SF19; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT C; 1.
DR PANTHER; PTHR32479; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190061};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 19..49
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 68..93
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 403 AA; 42613 MW; C1D89AC03D938CFC CRC64;
MSTAMPAPAS ARDGALPQVD VVVLADRCVQ CGLCLPACPT YRHDRLEADS PRGRIALAKA
WALDTIDPTP VGDAHMDGCL GCRSCEAVCP AGVEYGALLT LARANQRRRR GATTLQRLVE
WIVARPVLLA RLTAVYRQAR PWLPARLRFL PAPPAPVQPR PPEAGSPAPE SQAALFVGCI
AKGYEAPVRT ALSHLCLAVG VELATVPRQT CCGALHAHAG NQEAAERLAV VNRTAFTGHA
RVLTLASGCH DAVAAQVDGE TIDAIEFLQS RSDRLHFADA GGVRIALHLP CTQRNVVGSV
PALRRLLAAV PGLEVVELDA GFGCCGAAGT AMLTDPERAA EYRRPLLDQL AASGATRLLS
ANIGCRLHLA NGTTLPVQHP VEFLAERLSP RAHPFPATPE PVT
//
