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Database: UniProt
Entry: A0A1T1HD12_OCELI
LinkDB: A0A1T1HD12_OCELI
Original site: A0A1T1HD12_OCELI 
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
//
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