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Database: UniProt
Entry: X2H3L9_9NEIS
LinkDB: X2H3L9_9NEIS
Original site: X2H3L9_9NEIS 
ID   X2H3L9_9NEIS            Unreviewed;       304 AA.
AC   X2H3L9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Formate dehydrogenase O beta subunit {ECO:0000313|EMBL:AHN27999.1};
DE            EC=1.2.1.2 {ECO:0000313|EMBL:AHN27999.1};
GN   ORFNames=SALWKB2_0617 {ECO:0000313|EMBL:AHN27999.1};
OS   Snodgrassella alvi wkB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN27999.1, ECO:0000313|Proteomes:UP000019668};
RN   [1] {ECO:0000313|EMBL:AHN27999.1, ECO:0000313|Proteomes:UP000019668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WkB2 {ECO:0000313|EMBL:AHN27999.1};
RX   PubMed=25053814;
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "Genomics and host specialization of honey bee and bumble bee gut
RT   symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036298-50};
CC       Note=Binds 4 [4Fe-4S] clusters per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036298-50};
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DR   EMBL; CP007446; AHN27999.1; -; Genomic_DNA.
DR   RefSeq; WP_025330239.1; NZ_CP091515.1.
DR   AlphaFoldDB; X2H3L9; -.
DR   STRING; 1196094.SALWKB2_0617; -.
DR   GeneID; 32536976; -.
DR   KEGG; salv:SALWKB2_0617; -.
DR   PATRIC; fig|1196094.4.peg.617; -.
DR   HOGENOM; CLU_043374_0_3_4; -.
DR   OrthoDB; 9779457at2; -.
DR   Proteomes; UP000019668; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR   GO; GO:0015944; P:formate oxidation; IEA:InterPro.
DR   CDD; cd10558; FDH-N; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 1.20.5.480; Single helix bin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR006470; Formate_DH_bsu_Proteobacteria.
DR   InterPro; IPR038384; Formate_DH_C_sf.
DR   InterPro; IPR014603; Formate_DH_Fe-S_su.
DR   InterPro; IPR015246; Formate_DH_TM.
DR   NCBIfam; TIGR01582; FDH-beta; 1.
DR   PANTHER; PTHR43545; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, IRON-SULFUR SUBUNIT; 1.
DR   PANTHER; PTHR43545:SF4; FORMATE DEHYDROGENASE-O IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   Pfam; PF12800; Fer4_4; 1.
DR   Pfam; PF09163; Form-deh_trans; 1.
DR   PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036298-50};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036298-
KW   50}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036298-50};
KW   Oxidoreductase {ECO:0000313|EMBL:AHN27999.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          29..57
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          90..122
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          123..152
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         41
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         44
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         99
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         107
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         135
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         138
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         142
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         159
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         162
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         174
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
FT   BINDING         178
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036298-50"
SQ   SEQUENCE   304 AA;  33488 MW;  C38338CA61B94119 CRC64;
     MALQSLDIKR RSATNQLTPL PQARKPIEIA KLIDVSTCIG CKACQAACSE WNDIRDEVGT
     NHGVYDNPID LSADSWTVMR FSETEQYGKL EWLIRKDGCM HCSDPGCLKA CPSPGAIIQY
     ENGIVDFHQE NCIGCGYCIS GCPFNIPRIS KKDNRAYKCT LCSDRVAVGQ EPACVKTCPT
     GAIHFGSKED MKSLAGERIK DLKQRGFEQA GLYDPQGVGG THVMYVLHHA DKPSLYHGLP
     DNPRISTTVK LWKSMLKPIA AFGIATAAFA GWLHYITIGP NRPDDDKEQV LNREGEILKD
     KGDA
//
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