ID A0A0B4R9I8_9BACL Unreviewed; 440 AA.
AC A0A0B4R9I8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN ORFNames=Plano_0620 {ECO:0000313|EMBL:AIY04585.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY04585.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY04585.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY04585.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) 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; CP009129; AIY04585.1; -; Genomic_DNA.
DR RefSeq; WP_038702934.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4R9I8; -.
DR STRING; 1526927.Plano_0620; -.
DR KEGG; pln:Plano_0620; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_0_1_9; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000031496; 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: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 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:UP000031496};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 14..46
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 69..92
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 440 AA; 49221 MW; 436FF996D16BD034 CRC64;
MVVTELQQRM QQSFKENVDE EYLMDCMRCG FCLPACPTYL VTNKDEIHSP RGRIALMKGM
RDGDVVWDSS VKESFDMCLG CRACEPACPA GVQYGVLIEE TRVAIEQVKP QTIAEKAVRK
STFDGVFADQ KKMAGAVKLV QFYQKSGLQK ATRKIGFLNL FPPFMKEMEG VLPTIETKKK
RTAALKPKTT TVAFFAGCLM DTLFQETNRK TVELLESLGA NVVIPKEQQC CGALHGHSGE
LEKGLRNART NIDAFDSDSY DFIVNNAGGC GAFLSEYEKH LQVDSAYAEK SKRFSEKMID
ISSLLVKLGL NNRLKEIQVE SQAIVTYQDS CHLRNVNKVF LEPRSLLQDA PGFEYKELID
AESCCGSAGI YNILQPEMAK KILDLKMKGV KELQPAKVVT SNPGCLMQMQ VGIQREGLEK
EMQAVHIVDF LYDAIHKNQN
//
