ID A0A0N9IIK6_9PSEU Unreviewed; 835 AA.
AC A0A0N9IIK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ALG15284.1};
GN ORFNames=AOZ06_34710 {ECO:0000313|EMBL:ALG15284.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG15284.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG15284.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG15284.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-2015) 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; CP012752; ALG15284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N9IIK6; -.
DR STRING; 860235.AOZ06_34710; -.
DR KEGG; kphy:AOZ06_34710; -.
DR Proteomes; UP000063699; Chromosome.
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:UP000063699}.
FT DOMAIN 3..383
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 413..456
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 690..804
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 112..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 91999 MW; C4D7F51321530206 CRC64;
MAECHPVGFQ WVMAAKAKGA KIIHVDPRFT RTSAVSDVFV PIRAGSDIAF LGGLVNYVLT
HGKEFREYVV AYTNAAAIIT EEFKDTEDLD GLFSGFDAGK RAYDHSSWAY QGAEAQSGSG
DPGDRTGGEH QAAAQSEQHG SGGATIAAKP AEDPTLRHPR CVFQILKRHY ARYTPEMVEE
VCGVPVAKFL EVAEAITANS GRDRTTALCY AVGWTQHTVG VQYIRTASIL QSLLGNIGRP
GGGILALRGH ASIQGSTDIP TLFNILPGYI PMPHARQHLD LASFVANDAG RTGFWGNMDS
YTVSLLKSWW GEHATADNDF CFDYLPRLTG DHGTYSTVLR QIEGECKGYF LVGENPAVGS
ANGKLQRLGL ANLDWLVVRD LQMIESATFW RNGPEIETGE LRTEEIGTEV FFMPAAAHTE
KDGSFTNTQR LLQWHHKAVE PPGDARSDLW FYYHLGKLIR HKLRASKDPR DLPLQHLTWS
YVEEGPLGEP SAESVLAEIN GTGPDGPLSA YTELKNDGST ACGCWIYCGV RAGGENQAAR
RKPGREQTWV APEWGWAWPA NRRIIYNRAS ADPDGKPWSE RKRYIWWDAG QGKWVGEDVP
DFEGTKPPGF RPERGAKAQD GLGGDDPFIM QTDGKAWLFA PAGLADGPLP THYEPLESPY
SNPLYGQQAN PTLQRYDHPA NPCNGSAFPF VVTTYRLTEH HTAGAMSRTL PYLSELQPEF
FCEVSPELAE QQGLEHLGWA TIITSRTAIE ARVMVTQRMK PLRMRKQIVH QVGLPYHWGP
NGLSIGDAAN DILGVAADPN VHIQESKAAT CDIIPGRRPR GQALLDLVEE YRRRG
//