ID A0A150GMV5_GONPE Unreviewed; 932 AA.
AC A0A150GMV5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN ORFNames=GPECTOR_13g646 {ECO:0000313|EMBL:KXZ51159.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ51159.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ51159.1}.
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DR EMBL; LSYV01000014; KXZ51159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GMV5; -.
DR STRING; 33097.A0A150GMV5; -.
DR OrthoDB; 101479at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
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:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF10371; EKR; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SMART; SM00890; EKR; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 414..443
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 470..499
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 97966 MW; 8B564E1C32636693 CRC64;
MDIAKMPARL SKTAASHAGH LTAPTLLPGR GRRLVAKRLP AHSAVTAPHD GAAAADAARK
APAPSAIHHS NILPFSPAAP ASSAAPSAPP PAPACAKPSA PMDGNEAAAA IAYAVSDVAF
IYPITPATVM GELVDQWSAE GRRNAFGNVM SVTEMESETG AAGERAWALK AGRCKRAYFS
YDAHKSGGVT VSHLRFGPSR IRAPYLVQQA DYLAINHQSY MGKYDTLANL KPGGVVVINT
TFTNVESLGK YLPAKVKRQL AALRPQLHLI DAAAVARSSG LGKHVNMVMQ TVFFQLSGVL
PMERAVELLK KSIAKAYERK GPEVVAKNHA AVDAAISGLV KVAVPASWTE GVTAPVDPNP
PAKAAAGSRL AFLEQVAAPM LALEGDKLPV SVFEPEGFVP PGTTVIEKRA IAAQVPVWKA
ENCTQCNICA FVCPHAAIRP ALAAPAELAP APAGFGTVPA KGPGMGGLQY RIQVSPYDCT
GCDLCTHACP DDALALQPIE AVLQPESDNW EFARQLPVRS DLLDRHSVRG SQLQQPLMEF
SCACEGCGET PYVKLLTQLF GDRLVIANAT GCSSIWGGSA PSNPYTTNAA GFGPAWANSL
FEDNAQFGLG IATGIAQRRA SVHRQVTAAL ALAASQPVAL PLSPQLAAAL TRWAEHWQEP
AAANAAAAEA APLLAAEAAA ARGCAPLAAL AAQSDMLHKP STWIVGGDGW AYDIGFGGLD
HVLASGENVN ILVLDTEVYS NTGGQRSKAT PLSAVAKFAA GGKERPKKDL GAIAMSYGDV
YVATTSLQAN YGQVVRAMTQ AERYPGVSLL LCYAPCMLHG ISGGMCNAID ESKLAVETGY
WPLYRYDPSL PEGDAASGSR HRFQLDSKRL KGDVEALFQH ENRFQILARR DPDTAAAMHA
RLDAAVHSRH EHMKQLAAGE GAVAWGADRL QH
//
