ID D9PYF6_METTM Unreviewed; 281 AA. AC D9PYF6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 76. DE SubName: Full=F420-reducing hydrogenase, subunit beta {ECO:0000313|EMBL:ADL59254.1}; DE EC=1.12.98.1 {ECO:0000313|EMBL:ADL59254.1}; GN Name=frhB {ECO:0000313|EMBL:ADL59254.1}; GN OrderedLocusNames=MTBMA_c16830 {ECO:0000313|EMBL:ADL59254.1}; OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium OS thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929 {ECO:0000313|EMBL:ADL59254.1, ECO:0000313|Proteomes:UP000000345}; RN [1] {ECO:0000313|EMBL:ADL59254.1, ECO:0000313|Proteomes:UP000000345} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg {ECO:0000313|Proteomes:UP000000345}; RX PubMed=20802048; DOI=10.1128/JB.00844-10; RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., RA Gottschalk G., Thauer R.K.; RT "Complete genome sequence of Methanothermobacter marburgensis, a RT methanoarchaeon model organism."; RL J. Bacteriol. 192:5850-5851(2010). RN [2] {ECO:0007829|PDB:3ZFS} RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS). RX PubMed=23483797; DOI=10.7554/elife.00218; RA Mills D.J., Vitt S., Strauss M., Shima S., Vonck J.; RT "De novo modeling of the F(420)-reducing [NiFe]-hydrogenase from a RT methanogenic archaeon by cryo-electron microscopy."; RL Elife 2:e00218-e00218(2013). RN [3] {ECO:0007829|PDB:4CI0} RP STRUCTURE BY ELECTRON MICROSCOPY (3.36 ANGSTROMS) IN COMPLEX WITH FAD AND RP IRON-SULFUR (4FE-4S). RX PubMed=24569482; DOI=10.7554/ELIFE.01963; RA Allegretti M., Mills D.J., McMullan G., Kuhlbrandt W., Vonck J.; RT "Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo- RT microscopy using a direct electron detector."; RL Elife 3:e01963-e01963(2014). RN [4] {ECO:0007829|PDB:4OMF} RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH FAD AND [4FE-4S] RP CLUSTER. RX PubMed=24887099; DOI=10.1016/j.jmb.2014.05.024; RA Vitt S., Ma K., Warkentin E., Moll J., Pierik A.J., Shima S., Ermler U.; RT "The F-reducing [NiFe]-hydrogenase complex from Methanothermobacter RT marburgensis, the first X-ray structure of a group 3 family member."; RL J. Mol. Biol. 426:2813-2826(2014). CC -!- SIMILARITY: Belongs to the FrhB family. CC {ECO:0000256|ARBA:ARBA00038369}. 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; CP001710; ADL59254.1; -; Genomic_DNA. DR RefSeq; WP_013296464.1; NC_014408.1. DR PDB; 3ZFS; EM; 4.00 A; C=1-281. DR PDB; 4CI0; EM; 3.36 A; C=1-281. DR PDB; 4OMF; X-ray; 1.71 A; B=1-281. DR PDBsum; 3ZFS; -. DR PDBsum; 4CI0; -. DR PDBsum; 4OMF; -. DR AlphaFoldDB; D9PYF6; -. DR EMDB; EMD-2513; -. DR SMR; D9PYF6; -. DR STRING; 79929.MTBMA_c16830; -. DR PaxDb; 79929-MTBMA_c16830; -. DR GeneID; 9705394; -. DR KEGG; mmg:MTBMA_c16830; -. DR PATRIC; fig|79929.8.peg.1625; -. DR HOGENOM; CLU_037958_0_0_2; -. DR OrthoDB; 37898at2157; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 3.10.450.750; -; 1. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR045220; FRHB/FDHB/HCAR-like. DR InterPro; IPR017679; FrhB_archaea. DR InterPro; IPR007525; FrhB_FdhB_C. DR NCBIfam; TIGR03289; frhB; 1. DR PANTHER; PTHR31332; 7-HYDROXYMETHYL CHLOROPHYLL A REDUCTASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR31332:SF6; FORMATE DEHYDROGENASE SUBUNIT BETA; 1. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3ZFS, ECO:0007829|PDB:4CI0}; KW 4Fe-4S {ECO:0007829|PDB:4OMF}; FAD {ECO:0007829|PDB:4OMF}; KW Flavoprotein {ECO:0007829|PDB:4OMF}; Iron {ECO:0007829|PDB:4OMF}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0007829|PDB:4OMF}; KW Metal-binding {ECO:0007829|PDB:4OMF}; KW Nucleotide-binding {ECO:0007829|PDB:4OMF}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ADL59254.1}. FT DOMAIN 10..86 FT /note="Coenzyme F420 hydrogenase/dehydrogenase beta subunit FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF04422" FT DOMAIN 95..246 FT /note="Coenzyme F420 hydrogenase/dehydrogenase beta subunit FT C-terminal" FT /evidence="ECO:0000259|Pfam:PF04432" FT BINDING 24 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 25 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 27 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 28 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 29 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 30 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 48 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 71 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 73 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 74 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 75 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 77 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 104 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 134 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 135 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 192 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 195 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 198 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 209 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" FT BINDING 210 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4OMF" SQ SEQUENCE 281 AA; 30744 MW; 1E981B4ADF3B1A16 CRC64; MVLGTYKEIV SARSTDREIQ KLAQDGGIVT GLLAYALDEG IIEGAVVAGP GEEFWKPQPM VAMSSDELKA AAGTKYTFSP NVMMLKKAVR QYGIEKLGTV AIPCQTMGIR KMQTYPFGVR FLADKIKLLV GIYCMENFPY TSLQTFICEK LGVSMELVEK MDIGKGKFWV YTQDDVLTLP LKETHGYEQA GCKICKDYVA ELADVSTGSV GSPDGWSTVI TRTDAGDSIF KQAVEAGLFE TKPIEEVKPG LGLLEKLAAQ KKEKAEKNIA ARKEMGLPTP F //