ID A0A1J0VJL0_9GAMM Unreviewed; 951 AA.
AC A0A1J0VJL0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:APE32201.1};
GN ORFNames=BOX17_15320 {ECO:0000313|EMBL:APE32201.1};
OS Halomonas aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE32201.1, ECO:0000313|Proteomes:UP000181985};
RN [1] {ECO:0000313|Proteomes:UP000181985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA Koh H.-W., Rani S., Park S.-J.;
RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT from solar salt.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP018139; APE32201.1; -; Genomic_DNA.
DR RefSeq; WP_071946123.1; NZ_CP018139.1.
DR AlphaFoldDB; A0A1J0VJL0; -.
DR KEGG; hsi:BOX17_15320; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000181985; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 3.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 60..116
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 951 AA; 105965 MW; D215765A7AA91396 CRC64;
MRLTPKSDTP RPGGLGISRR QFLKRSGATT GGLAAAGFMG APMMQRAEAA EKTAWSDAPV
ETKRTVCSHC SVGCGVYAEV QEGVWTKQEP AFDHPINRGA HCAKGASLRQ HGHSSRRLKY
PMKLVGGQWQ RLSWEDAIEE IGDKVLSLTE QHGPDSIYWL GSAKFNNEQA YLMRKFAALA
GTNNTDHQAR ICHSTTVAGV ANTWGYGAMT NSLNDIQNSK SIMFIGSNPS EAHPVAMQHI
LLAKERSQAQ IIVVDPRFTR TAAKADSYVR IRPGSDVAFI WGLLWHIFEN GWEDSQYIEE
RVYAMDQVRA EVAAYSPDVV ENITGVPEDA MRDTARRLAE NRPGCVVWCM GGTQHTTGNN
NTRAYCILEL ALGNIGTSGG GANIFRGHDN VQGATDLGLM SHSLPGYYGL SEGAWKHWAR
VWDLDYEWLK GRFDQGDYVD GKPMYSSGIT VSRWIDGVLE QEEDISQRTR LKAMFYWGHA
VNSQTRGPEM QKAMQQLEMM VIVDPYPTVA GVMHDRQDGV YLLPAATQFE TYGSVTATNR
SIQWRDKVID PLFESKPDHE IMYLLSRKLG FADQLFKNVQ VNGTEPLIED LTREFNAGMW
TVGYTGQSPE RLKEHQQNWH TFSFRDLKAE GGPADGDYYG LPWPCWGTAE MGHPGTPILY
DTSKKVSEGG LTFRARFGIE RDGENLLADG SFSAGSELED GYPEFTDAML KDLGWWDDLT
DAEKAEAEGK NWKTDLSGGI QRVAIAHECA PFGNAKARCN VWTFPDPIPK HREPLYTSRR
DLVKEYPTWD DVASHYRLPT LYKTIQEKDV TGEYPIILTS GRLVEYEGGG EETRSMSWLA
ELQQEMFVEI NPALANDLAI TEGDMVWVEG AEGGRVKVKA LVTPRVAPEV VFMPFHFGGM
FQGESLHDRY PEGTAPYVLG EAANTATTYG YDSVTQMQET KCTLCRIEKA S
//
