ID A0A1T1HD12_OCELI Unreviewed; 954 AA.
AC A0A1T1HD12;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:OOV87706.1};
GN ORFNames=BTA35_0206725 {ECO:0000313|EMBL:OOV87706.1};
OS Oceanospirillum linum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oceanospirillum.
OX NCBI_TaxID=966 {ECO:0000313|EMBL:OOV87706.1, ECO:0000313|Proteomes:UP000190064};
RN [1] {ECO:0000313|EMBL:OOV87706.1, ECO:0000313|Proteomes:UP000190064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV87706.1,
RC ECO:0000313|Proteomes:UP000190064};
RA Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA Mykles D.L., Maclea K.S.;
RT "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT ATCC 11336.";
RL Submitted (FEB-2017) 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}.
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:OOV87706.1}.
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DR EMBL; MTSD02000002; OOV87706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1HD12; -.
DR STRING; 966.BTA35_0206725; -.
DR Proteomes; UP000190064; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000190064};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 64..120
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 954 AA; 106913 MW; 8FCCE7C8F2674598 CRC64;
MKLTKKNANG AGKADSKGLG LSRRTFLKNT GITTGGLAAA GFMGNGMIRQ AEAKTETISP
DVPKEVKRTI CSHCSVGCGV YAEVQNGVWT YQEPAFDHPF NRGAHCAKGA SLREHGHGER
RLKYPMKLVN GKWQKVSWET AIDEIGDKVQ QIRQESGPDS VYWLGSAKHS NEQAYLFRKF
ASLWGTNNVD HQARICHSTT VSGVANTWGY GAMTNSFNDM HNCKSVILIG SNPSEAHPVA
MQHVLLAKER NNAKIIVVDP RFTRTAAKAN EYVRIRPGSD VAYVWGLLWH IFENGWEDKE
FIRQRVYGMD EVRQEVANWT PAEVENVTGV GEEQMRKVAK MLATNRPGSI VWCMGGTQHT
TGSNNTRAYC ILMLALGNMG VSGGGANIFR GHDNVQGATD LGVLSHTLPG YYGLAAGAWK
HWAGVWDLDL EWIKSRFDQG KYRGKQPMYN SGIPVSRWVD GVLENKDQIE QKDNIRAMFY
WGHAVNSQTR GVEMKKAMEK LDMMVIVDPY PTHAAVMHDR KDGVYLLPAC TQFETYGSVT
ASNRSIQWRD QVIEPLFESK TDHEIMYRFA KKLGFADQLF KKIRVENNIP VIEDITREFN
SGMWTIGYSA QSPERLKDHQ KNWHTFDFET LKADGGAADG DFYGMPWPCW GTPEMRHPGT
PLLYDTSKPV AEGGLNFRAR FGVERDGVNL LAEDSYPVGA DIKDGHPEFS DKLLKQLGWW
DELTPEEKKA AEGKNWKTDL SGGIQRVAIK HGCAPFGNAK ARAVVWTFPD KVPLHREPLY
TPRRDLLSKY ATWKDVQSHY RLPTLYESIQ KQDFSKEYPI ILTSGRLVEY EGGGEETRSN
PWLAELQQEM FAEINPYDAN NLNVRDGADV WVEGAEGGRI KVKAMVTRRV DRGVVFIPFH
FGGKFQGKDL TDKYPQGSAP YVVGEAANTA TTYGYDSVTQ MQETKVTLCK VTPA
//