FER_METAC
ID FER_METAC Reviewed; 102 AA.
AC Q8TQQ5;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ferredoxin {ECO:0000303|PubMed:24214941};
GN OrderedLocusNames=MA_1485 {ECO:0000312|EMBL:AAM04899.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, COFACTOR, AND PATHWAY.
RX PubMed=24214941; DOI=10.1128/jb.00927-13;
RA Isobe K., Ogawa T., Hirose K., Yokoi T., Yoshimura T., Hemmi H.;
RT "Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans
RT are required for the synthesis of fully reduced archaeal membrane lipid in
RT Escherichia coli cells.";
RL J. Bacteriol. 196:417-423(2014).
CC -!- FUNCTION: Ferredoxin that is the specific electron donor for the
CC geranylgeranyl reductase GGR involved in the biosynthesis of archaeal
CC membrane lipids. {ECO:0000269|PubMed:24214941}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:24214941};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305|PubMed:24214941};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000305|PubMed:24214941}.
CC -!- MISCELLANEOUS: This ferredoxin is encoded just downstream from the GGR
CC gene in the genome of M.acetivorans. {ECO:0000305}.
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DR EMBL; AE010299; AAM04899.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TQQ5; -.
DR SMR; Q8TQQ5; -.
DR STRING; 188937.MA_1485; -.
DR EnsemblBacteria; AAM04899; AAM04899; MA_1485.
DR KEGG; mac:MA_1485; -.
DR HOGENOM; CLU_2271015_0_0_2; -.
DR InParanoid; Q8TQQ5; -.
DR PhylomeDB; Q8TQQ5; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 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:UniProt.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF00037; Fer4; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..102
FT /note="Ferredoxin"
FT /id="PRO_0000450803"
FT DOMAIN 45..73
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 74..102
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 102 AA; 11624 MW; EA79D280409613F3 CRC64;
MVWHYTNDVA LYCRAFRSMP HCLRERQYFM VKDHDLLLKL TGELVSVNIN RYKCGYCGAC
VGVCPKGALE LVETWIEVDE STCIKCGICD RICPVGAIEV MK
