ID MVHA_METTM Reviewed; 472 AA. AC P60227; D9PXZ8; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 02-SEP-2026, entry version 75. DE RecName: Full=F420-non-reducing hydrogenase subunit A; DE EC=1.12.99.-; DE AltName: Full=Methyl viologen-reducing hydrogenase subunit alpha; DE Short=MVH subunit A; GN Name=mvhA; OrderedLocusNames=MTBMA_c15170; OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium OS thermoautotrophicum). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; OC Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; 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] RP PROTEIN SEQUENCE OF 2-18, SUBUNIT, AND ASSOCIATION WITH HETERODISULFIDE RP REDUCTASE. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=8119281; DOI=10.1111/j.1432-1033.1994.tb18608.x; RA Setzke E., Hedderich R., Heiden S., Thauer R.K.; RT "H2: heterodisulfide oxidoreductase complex from Methanobacterium RT thermoautotrophicum. Composition and properties."; RL Eur. J. Biochem. 220:139-148(1994). RN [3] RP FUNCTION, AND ASSOCIATION WITH HETERODISULFIDE REDUCTASE. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=12856108; DOI=10.1007/s00203-003-0577-9; RA Stojanowic A., Mander G.J., Duin E.C., Hedderich R.; RT "Physiological role of the F420-non-reducing hydrogenase (Mvh) from RT Methanothermobacter marburgensis."; RL Arch. Microbiol. 180:194-203(2003). CC -!- FUNCTION: Part of a complex that provides reducing equivalents for CC heterodisulfide reductase. {ECO:0000269|PubMed:12856108}. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305}; CC -!- SUBUNIT: The F420-non-reducing hydrogenase is composed of three CC subunits; MvhA, MvhD and MvhG. It forms a complex with the CC heterodisulfide reductase (hdr). {ECO:0000269|PubMed:8119281}. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit CC family. {ECO:0000305}. 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; ADL59096.1; -; Genomic_DNA. DR RefSeq; WP_013296307.1; NC_014408.1. DR AlphaFoldDB; P60227; -. DR EMDB; EMD-55274; -. DR EMDB; EMD-55275; -. DR EMDB; EMD-55278; -. DR EMDB; EMD-55280; -. DR EMDB; EMD-55282; -. DR EMDB; EMD-55284; -. DR EMDB; EMD-55295; -. DR EMDB; EMD-55296; -. DR EMDB; EMD-55297; -. DR EMDB; EMD-55298; -. DR EMDB; EMD-55299; -. DR SMR; P60227; -. DR DIP; DIP-59603N; -. DR IntAct; P60227; 1. DR STRING; 79929.MTBMA_c15170; -. DR TCDB; 3.D.7.2.4; the h2:heterodisulfide oxidoreductase (hho) family. DR PaxDb; 79929-MTBMA_c15170; -. DR GeneID; 43707759; -. DR GeneID; 9705226; -. DR KEGG; mmg:MTBMA_c15170; -. DR PATRIC; fig|79929.8.peg.1470; -. DR HOGENOM; CLU_044556_0_0_2; -. DR OrthoDB; 42371at2157; -. DR BRENDA; 1.8.98.5; 7427. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR InterPro; IPR029014; NiFe-Hase_large. DR PANTHER; PTHR43600; COENZYME F420 HYDROGENASE, SUBUNIT ALPHA; 1. DR PANTHER; PTHR43600:SF2; F420-NON-REDUCING HYDROGENASE VHU SUBUNIT A; 1. DR Pfam; PF27537; HoxH; 1. DR Pfam; PF00374; NiFeSe_Hases; 2. DR SUPFAM; SSF56762; HydB/Nqo4-like; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. DR PROSITE; PS00508; NI_HGENASE_L_2; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Metal-binding; Nickel; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8119281" FT CHAIN 2..472 FT /note="F420-non-reducing hydrogenase subunit A" FT /id="PRO_0000199727" FT BINDING 61 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000255" FT BINDING 64 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000255" FT BINDING 442 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000255" FT BINDING 445 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /evidence="ECO:0000255" FT CONFLICT 11 FT /note="R -> L (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 472 AA; 52839 MW; 5993E7AC4BC0579F CRC64; MVKLTMEPVT RIEGHAKITV HLDDAGNVED TRLHVMEFRG FEKFLQGRPI EEAPRIVPRI CGICDVQHHL AAAKAVDACF GFEPDDVLPA AYKMREIMNW GSYMHSHGLH FYFLAAPDFI AGKDRKTRNV FQIIKDAPDV ALQAIELRKN ALEIVRATGG RPIHPTSSTP GGISTELDDE TQKDLLQKAQ RNVELAEATL ELAVPIFEEN IDLVNSLGNI ETYHTGLVKN GVWDVYDGIV RIKDKEGNLF REFKPADYAD TIAEHVKPYS WLKFPYIKDL GYPDGVYRVS PLSRLNVADK MPDAAPKAQD YFKEFQDKFG YAQQTLLYHW ARLIEVLACA ECAADALEGD LSGEKFPDSL ERQAGDGVGI VEAPRGTLTH HYTCDENGLI TKANIVVATI QNNPAMEMGI QKVAQDYIKP GVEVDDKIFN LMEMVIRAYD PCLSCATHTI DSQMRLATLE VYDSEGDLVK RI //