ID A0A0D1CSS0_9RHOB Unreviewed; 467 AA.
AC A0A0D1CSS0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 {ECO:0000313|EMBL:KIT17802.1};
GN ORFNames=jaqu_03910 {ECO:0000313|EMBL:KIT17802.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT17802.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT17802.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT17802.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
RL Submitted (FEB-2015) 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:KIT17802.1}.
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DR EMBL; JYFE01000013; KIT17802.1; -; Genomic_DNA.
DR RefSeq; WP_043917258.1; NZ_JYFE01000013.1.
DR AlphaFoldDB; A0A0D1CSS0; -.
DR STRING; 935700.jaqu_03910; -.
DR PATRIC; fig|935700.4.peg.420; -.
DR OrthoDB; 9765258at2; -.
DR Proteomes; UP000032232; 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: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:UP000032232};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 14..46
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 66..96
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50510 MW; FC87FE6B12C9E78B CRC64;
MQTTFTPAQL TDPATARSNE ILRACVHCGF CTATCPTYQV LGDELDSPRG RIYLIKQMLE
EGRPADAQTV KHIDRCLSCL ACMTTCPSGV HYMHLVDHAR EYIEQTYTRP WHDRALRWVL
AQILPYPMRF RVALLGAKIG KPFARLMPDA RLRAMLAMAP DTIPPVSRND DPQTFAVPER
KMRVALMTGC AQKALNTDIN DATIRLLTRL GAEVVVAEGA GCCGALTHHM GKTEESHRFA
AANIEAWHRE MQGDGLDAIV INTSGCGTTV KDYGHMFRSD PLAEKAAAIA GLAKDVSEVL
VDLLPADFPF ETPPRPAKTG IAGVPTSRRP DAEGQGPMRV AYHAACSLQH GQKIKAAPKD
LLKRAGFEVV EPRDSHLCCG SAGTYNLMQP EISGELKARK VATLEERAPD VIAAGNIGCM
MQIGSAASAP VVHTVELLDW ATGGPVPPAI ESVSGQMPKA PAVPKLR
//
