VHCD_ARCPA
ID VHCD_ARCPA Reviewed; 137 AA.
AC P84624; D2REQ4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=F420-non-reducing hydrogenase iron-sulfur subunit D;
DE EC=1.12.99.-;
GN Name=mvhD; OrderedLocusNames=Arcpr_1552;
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18;
RX PubMed=21304717; DOI=10.4056/sigs.942153;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-20, COFACTOR, INTERACTION WITH HETERODISULFIDE
RP REDUCTASE, AND SUBCELLULAR LOCATION.
RX PubMed=15009189; DOI=10.1111/j.1432-1033.2004.04013.x;
RA Mander G.J., Pierik A.J., Huber H., Hedderich R.;
RT "Two distinct heterodisulfide reductase-like enzymes in the sulfate-
RT reducing archaeon Archaeoglobus profundus.";
RL Eur. J. Biochem. 271:1106-1116(2004).
CC -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC heterodisulfide reductase. MvhD may form the contact site for
CC heterodisulfide reductase. {ECO:0000269|PubMed:15009189}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:15009189};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:15009189};
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:15009189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15009189}.
CC -!- SIMILARITY: Belongs to the MvhD/VhuD family. {ECO:0000305}.
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DR EMBL; CP001857; ADB58598.1; -; Genomic_DNA.
DR RefSeq; WP_012940934.1; NC_013741.1.
DR AlphaFoldDB; P84624; -.
DR SMR; P84624; -.
DR STRING; 572546.Arcpr_1552; -.
DR EnsemblBacteria; ADB58598; ADB58598; Arcpr_1552.
DR GeneID; 8740242; -.
DR KEGG; apo:Arcpr_1552; -.
DR eggNOG; arCOG02475; Archaea.
DR HOGENOM; CLU_095272_2_0_2; -.
DR OMA; FPCTGRI; -.
DR OrthoDB; 91498at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003813; MvhD/FlpD.
DR Pfam; PF02662; FlpD; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..137
FT /note="F420-non-reducing hydrogenase iron-sulfur subunit D"
FT /id="PRO_0000218276"
FT CONFLICT 10..14
FT /note="VCIAC -> IVAA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15486 MW; FFB9EEDD5D2130A6 CRC64;
MSEEWEPNIV CIACNWCTYQ AADMAGSLRY SYPPTVKVVR VPCSGRVEPE FIVEALTNGA
DGVIVGGCHL GDCHYKEGNY KALRRFKLLH KLLTELGIEP ERVRLEWISG SEGLKFAEVM
TEFDATIRKL GPFKFER
