ID A0A1Q5JAA0_9ACTN Unreviewed; 897 AA.
AC A0A1Q5JAA0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:OKJ66148.1};
GN ORFNames=AMK29_15740 {ECO:0000313|EMBL:OKJ66148.1};
OS Streptomyces sp. CB02261.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ66148.1, ECO:0000313|Proteomes:UP000186742};
RN [1] {ECO:0000313|EMBL:OKJ66148.1, ECO:0000313|Proteomes:UP000186742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02261 {ECO:0000313|EMBL:OKJ66148.1,
RC ECO:0000313|Proteomes:UP000186742};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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:OKJ66148.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIVX01000004; OKJ66148.1; -; Genomic_DNA.
DR RefSeq; WP_073813277.1; NZ_LIVX01000004.1.
DR AlphaFoldDB; A0A1Q5JAA0; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000186742; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; 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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
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 NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 132..163
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 176..204
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 215..271
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 897 AA; 94066 MW; 8774C165F63AD7F1 CRC64;
MTRLQVDGVP VELPAGASLL DAVRAIGAEL PTLCHDDRLR SAGSCRTCLV RADGRTVAAC
VTPATSGLTV DTADEGVRNL RRDAVALIAS ALPPHALADS AHSELAEACR ALGIPVDSAA
GEPTRGRDES HPYVHLDRDL CIACGRCVRM CSDVQGTFAL TLIGRGADTV VSPGTGGPWA
DSDCVSCGGC VDTCPTGAIT GPGPGQGLTS RRVPADRTRT TCGYCGVGCT LDVVVREDRV
AAVLPARDGP VNRGHACVKG RFAYGYLGSA ERLTEPLIRE NGELRPATWD EAVTRIADGL
RAAVLDGGPD AVAAISSARA ANEENYLVQK LLRAVIGTNN VDNCSRLCHA PSAAGLTASF
GRAGGTDPFD DVETADCLMV VGANPVEAHP VVGARLLQRA LAGASLIVAD PRAVGLARHA
DVHLRPRPGT NVALFHGLAH VLVDEGMTDP GFLHDRAIGL DELADLLADY PPARVARITG
VPAADIRTAA RLYGLAERPA VLYGLGVTEH LHGTDGVRTL ANLPILRGAV GGTGRGFGIS
PLRGQNNVQG ASDMGALPDL LPGYGRVTDP EARARAEAVW GRPVSPTPGL RIPEMFAAAR
EGRLRALWII GEDVCATDPD SRRVAEALDA CPLVVVNELF LGETARHADV VLPVASWLEK
DGTFVNFDRR FQRVRQAVKP PGTARSDFGV VHAVADALGA DLGCPTPAAA LAECGRVTPL
FAGLSHERLD REGAVPWPCP APDRPGEATL YVEGFATPDG RAHLSAAPYL PPGEEPDHDY
PLVLVTGRRW AHYNSGSMTR RGGNLLLDAS DPLDLHPEDA ARFGIRDGSP VTVESRHGLA
RLVARVGMEL APGQVFCAFH FPASAVNSLT SEHADTVTSC PEYKVTAVRL RPTVSDD
//
