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Entry: A0A0F7KJ61_9PROT
LinkDB: A0A0F7KJ61_9PROT
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ID   A0A0F7KJ61_9PROT        Unreviewed;       430 AA.
AC   A0A0F7KJ61;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE            EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN   ORFNames=AAW31_15840 {ECO:0000313|EMBL:AKH38939.1}, BCL69_104622
GN   {ECO:0000313|EMBL:TYP82112.1};
OS   Nitrosomonas communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH38939.1, ECO:0000313|Proteomes:UP000034156};
RN   [1] {ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Draft genome of Nitrosomonas communis strain Nm2.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKH38939.1, ECO:0000313|Proteomes:UP000034156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:AKH38939.1,
RC   ECO:0000313|Proteomes:UP000034156};
RX   PubMed=26769932;
RA   Kozlowski J.A., Kits K.D., Stein L.Y.;
RT   "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT   Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL   Genome Announc. 4:0-0(2016).
RN   [3] {ECO:0000313|EMBL:TYP82112.1, ECO:0000313|Proteomes:UP000324176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm2 {ECO:0000313|EMBL:TYP82112.1,
RC   ECO:0000313|Proteomes:UP000324176};
RA   Wagner M.;
RT   "Active sludge and wastewater microbial communities from Klosterneuburg,
RT   Austria.";
RL   Submitted (JUL-2019) 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; CP011451; AKH38939.1; -; Genomic_DNA.
DR   EMBL; VNHT01000046; TYP82112.1; -; Genomic_DNA.
DR   RefSeq; WP_046850973.1; NZ_VNHT01000046.1.
DR   AlphaFoldDB; A0A0F7KJ61; -.
DR   KEGG; nco:AAW31_15840; -.
DR   PATRIC; fig|44574.3.peg.3833; -.
DR   Proteomes; UP000034156; Chromosome.
DR   Proteomes; UP000324176; 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   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; 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:UP000034156};
KW   Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT   DOMAIN          14..43
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          65..96
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   430 AA;  47783 MW;  780AE553E29DF255 CRC64;
     MHTKNDSLIK SSRSSLLAEA NRCVSCGLCL PHCPTYRLTL SEADSPRGRI AMISGVASQR
     IPMNARFAEH IDRCLTCRAC EAACPSQVAY GQLIDEARDM LTASLSDLPE ERVIRKKNGF
     KSWLEKIFID KTKRFDLLRP LIHLFQAVGL QEKLQQSSKV KGTKLGLLLS KLSLIRFPFH
     RWQEVYPAMG RKRGEVALFL GCVARLVDAE TSISAIFVLN HLGYTVYVPR AQTCCGALYQ
     HSGRLTKAAY LIERNRKVFA GLNIHAIIST ASGCGSHLVE SCSQHQGKNF SAPIMDINQF
     LAEQDWSEVK LRALPKKVVV HDPCSMRNGL RASIYPYQLL ARIPDIEILE LDGNNFCCGA
     AGTYFLDQPE IAEVLLNDKM RALAQSVETS YLVTSNIGCL LHLASGLSNQ EEKVEVLHPV
     TLLARQIGIQ
//
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