ID Q2RJ81_MOOTA Unreviewed; 1487 AA.
AC Q2RJ81;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=4Fe-4S ferredoxin, iron-sulfur binding protein {ECO:0000313|EMBL:ABC19508.1};
GN OrderedLocusNames=Moth_1194 {ECO:0000313|EMBL:ABC19508.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19508.1};
RN [1] {ECO:0000313|EMBL:ABC19508.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19508.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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DR EMBL; CP000232; ABC19508.1; -; Genomic_DNA.
DR RefSeq; YP_430051.1; NC_007644.1.
DR STRING; 264732.Moth_1194; -.
DR EnsemblBacteria; ABC19508; ABC19508; Moth_1194.
DR KEGG; mta:Moth_1194; -.
DR PATRIC; fig|264732.11.peg.1282; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1148; Bacteria.
DR HOGENOM; CLU_004231_0_0_9; -.
DR OrthoDB; 10014at2; -.
DR BioCyc; MetaCyc:MONOMER-18819; -.
DR GO; GO:0051536; F:iron-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:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 3.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 105..135
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 1412..1441
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 1442..1471
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 571..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 162758 MW; 42CB53411382B2B5 CRC64;
MSAKKETTPA VGAVLVLGGG IAGMQSALDL ANAGYLVHMV TESSSIGGHM AQLDKTFPTN
ECAMCLLGPR MTDTSNHPNI RLHTCATLEK VEGEKGNFTV QIREKPRYVN IQECTACGDC
EQACPVSIPN EYNQEMGTRK AIHKMFPQAV PNKYLITKRG TPPCRSTCPA GTNVQGYVAL
ISQGKFAEAL EVVHRRMPFA GICGRICHHP CETECNRGRY DDPIAIATLK RAAYDYGWEA
EASREKERRP ELPSRKEKVA IIGAGPAGLT AAQDLALAGY QVTIYDALNQ PGGMLRGGIP
RYRLPMEVVD RETQRILNLG IKFVPNTVVG KDINLKDLQK EYNAVIIAVG LQQSRMLKLD
GSELEGILPG VNFLREAALG GRPEVGEKVV VIGGGNVAID VARTARRLGA REVHLACLES
REEMPAHPWE VEEALEEGII LHPSWGPKRF LGAKGRVTGI ELMQCTRVFD EEHRFNPQYN
PEVTQTLTAD TIIMAIGQAA DLSLLGEKSP VATNRGLIKA DPLTLATSVP GVFACGDIVR
GPASVVEAVA SGHEAAESVK RYLQGEDLAT GRSLEKEPHL DPPPNVVPFP GRRQAQAMAP
VEERVKDFRE VYQGFTPEEA IAEAKRCLNC GICSECLQCE AVCKKKAIEH WQQEKVTKLK
VGSIVLAPGF ELFDATLAGE YGYGYYANVL TSLEFERLLS ATGPTESHVL RPSDQRPPKK
VAFIQCVGSR DCEREGSPYC SAICCMYSTK EALIAREHDA NIEPTIFYLD IRAYGKNFDR
YVESAKAGGV RYVRAMISRV EEDPQTKNLI IQYYTDGRVQ REEFDLVVLA VGVKPPIDAE
KIAAATGIEL NPYGFAKTQP FEPVATTRDG IYVAGVFQGP RDIPETVVNA SAAAACAGAA
MAPGRNTMIT PKEYPPERDV SREEPRVGVF ICHCGINIAG VVDVKAVVEA AAKLPGVVHA
EDNLYTCSQD TLKKIKDAIQ EYRLNRVVVA SCTIRTHQPL FREALREAGL NQFYFEMANI
RDQCSWVHRN EPANATLKAI DLVRMAVAKV KRHEALHLQP VPVIQKALII GGGVAGLTAA
LNVAEQGFEA YIVEREAELG GQVRNLRTTL EGEDLQALLR DLITRVQANP RIQVFTRARI
EDFGGHQGHF TTTISLGEPG REHVRRTQTL EHGVVIVATG SQEIKTDAYL LGQDERVITN
TRLEQALADG HWDQEKNKQV VFIQCVGSRD QEHPYCSRTC CAQTIKNALA IKRRNPEAQV
YVLYRDIRTY AFMEDYYRQA REAGVLFIAY DPGDPPRVRQ REIGLLEVMV KDPDSGKELV
LWPDQLVLAT GAVAPDGVEE LASLLKLPLN EDRFYVETHA KLAPIDFPTA GIFLCGAGHA
PKLAAEAIAQ AEGAVARACT ILARENLMVG GVVAVVDENK CAACLTCVRV CPFNVPRINE
RNVAEINAVQ CMGCGTCAGE CPAKAIQLQF YKDDQLLAKV AGLFGEV
//
