ID A0A150J954_9EURY Unreviewed; 1185 AA.
AC A0A150J954;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Pyruvate synthase subunit PorA {ECO:0000313|EMBL:KYC53782.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:KYC53782.1};
GN Name=porA {ECO:0000313|EMBL:KYC53782.1};
GN ORFNames=AMQ74_00282 {ECO:0000313|EMBL:KYC53782.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Candidatus Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC53782.1, ECO:0000313|Proteomes:UP000075578};
RN [1] {ECO:0000313|EMBL:KYC53782.1, ECO:0000313|Proteomes:UP000075578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin089 {ECO:0000313|EMBL:KYC53782.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000256|ARBA:ARBA00011595}.
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:KYC53782.1}.
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DR EMBL; LNGD01000009; KYC53782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150J954; -.
DR PATRIC; fig|1705564.3.peg.282; -.
DR Proteomes; UP000075578; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR CDD; cd03377; TPP_PFOR_PNO; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR033412; PFOR_II.
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; IPR011895; Pyrv_flavodox_OxRed.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR02176; pyruv_ox_red; 1.
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; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF000159; NifJ; 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 SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KYC53782.1}; Pyruvate {ECO:0000313|EMBL:KYC53782.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 683..712
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..769
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1185 AA; 131902 MW; 59E8147B9CBCA611 CRC64;
MVTIDGNEAA AYTAYHVNEV ISIYPITPSS TMGELSDQWA SEGKPNIWGS VPHVTEMQSE
AGAAGAVHGS LQRGALTTTF TASQGLLLMI PNMYKIAGEL TSTVFHVSAR TLATHALSIF
CDHGDVMSVR STGFALLVSN SVQEVMDLAL IAHASTLKSR VPFLHFFDGF RTSAEVSKVE
LLSFEDMKQM IDDELVREHR SRALSPDNPI IRGTSHNPDT FFQAKETINP YYNSCPEIVQ
EMMDKFEKIV GRKYKLFDYV GAPDAERIIV IMGSGAETVE ETVDYLKMKG EKVGVIKVRL
FRPFSIKHFV SSLPKSVKSI AVLDRTKEPG SVGEPLYLDV TTAIASALSD GTLKMDKMPK
IIGGIYGLSS KEFKPSMVKA VFDELKKINP KSKFTVGIND DVTHLSLDYD PNFFIEPTNR
TRAVFFGIGS DGTVSANKST IKIIGEETNN YAQGFFYYDS KKAGSQTLSH LRFGPDPIRS
PYLIDKANFV ACHQSSFLDR YEMLNVAEPN AIFLLNSTYS KDEVWDHLPK SVQKEIIDKN
LKFYVIDAYK IAKEIGLGVR INTIMQTCFF ALSNVIPRDE AIKKIKKFTE KTYGLKGEKI
LNMNYEAIDK AIDNLHQVNV PKKVSSEFDL KTSMPEDAPP FVKNAISKMV IGKGNELPVS
AFPSDGTYPT GTTKWEKRNI SLEVPVWDPS ICIQCGKCVF ACPHAVIRAK VYTKDALKNA
PPSFKYTEAK FSQFKDYLYT VQASPEDCTG CKICHEVCPS KNKQDPKLKA VNMVFKDSIL
AREKNNWDFF DSIPYVDRDK LNFTAVKDIQ LLQPLFEFSG ACSGCGETPY VKLLTQLFGD
RAVIANATGC SSIYGGNLPT TPYTTNKDGR GPTWSNSLFE DTAEFGLGMR LALDKQYEYA
LELLDKLKED LSKDLIFELK NADQKTEAGI NKQREMVKLL KAKLKGIQKP EAKDLLSLAD
SLVKKSVWII GGDGWAYDIG YGGLDHVLAQ GKNVNILVLD TEVYSNTGGQ KSKATPIGAI
AKFAMGGKAT PKKDLAMMAM NYGNVYVARV AFGANNAQTI KAFLEAESFE GTSIIIAYSH
CTQHGYDMIR GPDQQKAAVM SGYWPLIRYD PRLSDQGKNP FQLDSAKPSI PLQDYIYNET
RFKVLTRSHP DVAKKLLGYA QKEVNKRWNL YKYWADMPPF KEEDK
//