ID A0A1H8XCC1_9PSEU Unreviewed; 851 AA.
AC A0A1H8XCC1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SEP37463.1};
GN ORFNames=SAMN04489732_10714 {ECO:0000313|EMBL:SEP37463.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP37463.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP37463.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP37463.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FOEF01000007; SEP37463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XCC1; -.
DR STRING; 394193.SAMN04489732_10714; -.
DR Proteomes; UP000198582; Unassembled WGS sequence.
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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR NCBIfam; NF041513; formate_DH_Act; 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; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 3..390
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 420..461
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 699..816
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 114..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 93337 MW; 4A62AE399B467846 CRC64;
MAECHPVGFQ WVMEAKARGA KIIHVDPRFT RTSAVSHVHA ALRAGTDIAF LGGLINHVLR
NGLDFREYVL AYTNAAAILT EEFADTEDLD GLFSGYDPEK RQYDISTWAY EDADATPAAG
SGEPEQSGEH HHGGERHQRA ARGESYGSGG ASVHAKPKTD ETLQHPRCVY QVLKRHFARY
TPEAVADICG LPVEQFAEIA EAVTANSGRE RTTAWVYSVG WTHHTVGAQY IRTASILQTL
LGNIGRPGGG ILALRGHASI QGSTDIPTLF NLLPGYIPMP HAHEHFDLDG FVAADAGKTG
FWGNMRAYTV SLLKAYWGES AQPGNDFRFD YLPRLTGDHG TYATVQQQIE GECKGYFLVG
ENPAVGSANG KFQRLGLANL DWLVVRDLQL IESATFWKNG QEIETGELAT TEIGTEVFFL
PAAAHTEKDG SFTNTQRLLQ WHHKAVEPPG EARSDLWFYY HLGRLIRERI GDDPRDAPLR
DLTWSYPTAG PTADPSAESV LAEINGHGPD GPLAAYTELK DDGSTTCGCW IYCGVRADGH
NHAADRKPGS EQDWVAGGWA WAWPANRRIL YNRASADPDG KAWSERKKLI TWDAGQGRWV
GPDVPDFEVT KPPDYVPPEG AKAQAALGGA DAFIMQTDGK AWLFAPAGLA DGPLPAHYEP
FESPVGNALY SQQESPTRQT LDSPHNRYNP ARSKAYPYVF TTYRLTEHHT AGGMSRTLPY
LAELQPEFFC EVSPALAAER GLEHLGWATI VSARTAIEAR VLVTDRIKPL KVRGRTIHQV
GLPYHWGPNG LSRGDAANDL LSVVMDPNVH IQEAKAATCD IRPGRRPRGP ALPVHVEEYR
SRAEEGEPTD G
//