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Database: UniProt
Entry: A0A0W0TWE3_9GAMM
LinkDB: A0A0W0TWE3_9GAMM
Original site: A0A0W0TWE3_9GAMM 
ID   A0A0W0TWE3_9GAMM        Unreviewed;       278 AA.
AC   A0A0W0TWE3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Hydrogenase/sulfur reductase gamma subunit {ECO:0000313|EMBL:SPX60496.1};
DE   SubName: Full=Hydrogenase/sulfur reductase subunit gamma {ECO:0000313|EMBL:KTC99774.1};
GN   Name=hydG-2 {ECO:0000313|EMBL:KTC99774.1};
GN   Synonyms=pyrK {ECO:0000313|EMBL:SPX60496.1};
GN   ORFNames=Lfee_1335 {ECO:0000313|EMBL:KTC99774.1}, NCTC12022_01227
GN   {ECO:0000313|EMBL:SPX60496.1};
OS   Legionella feeleii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=453 {ECO:0000313|EMBL:KTC99774.1, ECO:0000313|Proteomes:UP000054698};
RN   [1] {ECO:0000313|EMBL:KTC99774.1, ECO:0000313|Proteomes:UP000054698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-44C {ECO:0000313|EMBL:KTC99774.1,
RC   ECO:0000313|Proteomes:UP000054698};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SPX60496.1, ECO:0000313|Proteomes:UP000251942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX60496.1,
RC   ECO:0000313|Proteomes:UP000251942};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
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DR   EMBL; LNYB01000049; KTC99774.1; -; Genomic_DNA.
DR   EMBL; UASS01000010; SPX60496.1; -; Genomic_DNA.
DR   RefSeq; WP_058445145.1; NZ_UASS01000010.1.
DR   AlphaFoldDB; A0A0W0TWE3; -.
DR   STRING; 453.Lfee_1335; -.
DR   PATRIC; fig|453.4.peg.1448; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000054698; Unassembled WGS sequence.
DR   Proteomes; UP000251942; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd06221; sulfite_reductase_like; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR   PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054698}.
FT   DOMAIN          6..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         242
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         247
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         250
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         258
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   278 AA;  30710 MW;  E6FF9458C321670C CRC64;
     MIRDSYLPRT ARIKARHQES ATIFTLDLQF VEKSHQQAFS FYPGQFNMLY LYGVGEVAIS
     ISSDPAEKTY LGHTIRAVGR VTKAMQQLNK GDYVGVRGPF GNGWPVKGAV GKDIVIVTGG
     LGCAPTVSVI NYILARREQY GALKIFQGVK HSEDFIFRKQ YKKWQAMPQT EIYIAADKAG
     PKWPWSVGYV TDMITSLQLD ANNTIAMMCG PEGMMQAATL ALINQGISGE AIYLSMERNM
     ECGIGHCGHC QYGGLFVCKD GPVFAYDCIK ALFTEPGF
//
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