ID A0A165FVI0_9NEIS Unreviewed; 412 AA.
AC A0A165FVI0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glycolate oxidase iron-sulfur subunit {ECO:0000256|PIRNR:PIRNR000139};
DE EC=1.1.99.14 {ECO:0000256|PIRNR:PIRNR000139};
GN Name=glcF {ECO:0000313|EMBL:KZE34322.1};
GN ORFNames=AVW16_06515 {ECO:0000313|EMBL:KZE34322.1};
OS Crenobacter luteus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Crenobacter.
OX NCBI_TaxID=1452487 {ECO:0000313|EMBL:KZE34322.1, ECO:0000313|Proteomes:UP000076625};
RN [1] {ECO:0000313|Proteomes:UP000076625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN10 {ECO:0000313|Proteomes:UP000076625};
RA Hong K.W.;
RT "Draft genome of Chromobacterium sp. F49.";
RL Submitted (JAN-2016) 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:KZE34322.1}.
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DR EMBL; LQQU01000008; KZE34322.1; -; Genomic_DNA.
DR RefSeq; WP_066610214.1; NZ_LQQU01000008.1.
DR AlphaFoldDB; A0A165FVI0; -.
DR STRING; 1452487.AVW16_06515; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000076625; 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; 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:UP000076625};
KW Transport {ECO:0000256|PIRNR:PIRNR000139}.
FT DOMAIN 11..44
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 66..89
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 412 AA; 44514 MW; C95B302E24D02D72 CRC64;
MQTRLADFIK DTPEGVDADA ILRRCVHCGF CTATCPTYQE LGDELDGPRG RIYLIKQVLE
GAPATAKTQS HLDRCLSCRN CESTCPSGVE YGRLLDIGRH VVDAQVKRPL GARIVRRALA
TVLPNPRLFG PAYRLGQRLR PLLPASLKAK LLPQSDAGAA PPRRAHARKV LMLAGCVQPV
MLPNINHATL RVLDALGIEA ILPADAGCCG ALRYHLDEQD AGLADMRRNV DAWWPHIEAG
VEAIVVNASG CGVAVKEYGR YLRHDPAYAD KAARVSALAR DLVEIVAPEA ANLAARVAAS
PLRRVAYHPP CTLQHGQRVR GQLEKLLQTL GLAVLLPTDS HLCCGSAGTY SLLQPELSLK
LRDNKLAALA RTTPDLIVSG NVGCIGHLRG GTATPVMHWV ELVDRMLTDT AR
//
