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Database: UniProt
Entry: Q31MH2_SYNE7
LinkDB: Q31MH2_SYNE7
Original site: Q31MH2_SYNE7 
ID   Q31MH2_SYNE7            Unreviewed;       433 AA.
AC   Q31MH2;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   OrderedLocusNames=Synpcc7942_1717 {ECO:0000313|EMBL:ABB57747.1};
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB57747.1, ECO:0000313|Proteomes:UP000889800};
RN   [1] {ECO:0000313|Proteomes:UP000889800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC   {ECO:0000313|Proteomes:UP000889800};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB57747.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31MH2; -.
DR   STRING; 1140.Synpcc7942_1717; -.
DR   PaxDb; 1140-Synpcc7942_1717; -.
DR   KEGG; syf:Synpcc7942_1717; -.
DR   eggNOG; COG0247; Bacteria.
DR   HOGENOM; CLU_023081_0_1_3; -.
DR   BioCyc; SYNEL:SYNPCC7942_1717-MONOMER; -.
DR   Proteomes; UP000889800; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000889800};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          11..40
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          60..92
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   433 AA;  48049 MW;  59BA7151AEDD333E CRC64;
     MAETEIPIPA ATPSLTDACV HCGFCLSDCP SYRVLGRETD SPRGRVYLMD SLQQGRIELS
     DTVVEHFDTC LGCLACTSAC PSGVQYDQLI EEMRQRIAQE HRRPWPEAIW RKLLFAFLPY
     PERLRPILRL GQLYQSSGLQ NWLNRQPLLQ KFPQLAAASA LLPPLSPASF QDNWPTLLPA
     LGDRRYRVGL LLGCVQRLFN PEVNAAAIRV LRANGCDVVI PPQQGCCGAV AHHQGEMQQA
     QDLARAVIRS FEAENLDAIL VTASGCGHTL KHYGAILADD PEWCDRAQQL ADRVQDVQEF
     LATVGLTTPL HPLQEQPLVV VYQDACHMLH GQKIRNQPRQ LLQQIPGIEL REPVDAQLCC
     GSAGIYNLLQ PAIAAELGQQ KARSLAETGA QMIASANIGC YVQIRHHLQA QSKDLPVLHP
     LQIIDRAMNF QNH
//
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